Prof. H.S. Subramanya

Prof. H.S. Subramanya

Ph.D., Indian Institute of Science, Bengaluru; Post-doc, Oxford University, UK
Pro Vice-Chancellor

Prof. H.S. Subramanya

Ph.D., Indian Institute of Science, Bengaluru; Post-doc, Oxford University, UK
hosahalli_s@chanakyauniversity.edu.in
Structural Biology, Drug Discovery, X-Ray Crystallography, Drug Targets

My principal research interests are in the interface of structural biology, molecular function, and drug discovery. Proteins and their three-dimensional architectures govern virtually all cellular processes. Understanding how structure dictates function remains central to addressing pressing biomedical challenges. Over the last three decades, rapid advances in structural biology techniques, particularly X-ray crystallography, cryo-electron microscopy (cryo-EM), and integrative structural bioinformatics, have significantly increased our capability to visualize macromolecules at an atomic resolution. However, integrating structural findings into novel therapeutic techniques remains a challenging scientific field.

My research elucidated structure–function relationships of biologically and clinically relevant proteins. I further utilized this knowledge to guide the design and development of targeted drug molecules. Proteins that play pivotal roles in cancer, infectious diseases, and metabolic disorders are inherently dynamic and complex. Dissecting how subtle structural changes modulate activity, ligand binding and enzymatic mechanism is fundamental to creating highly specific drug molecules with improved efficacy and reduced off-target effects.

Prof. H. S. Subramanya is the Pro-Vice Chancellor of Chanakya University as well as the Dean of the School of Biosciences at Chanakya University. He is a structural biologist whose research focuses on understanding protein structure-function relationships and applying this knowledge to rational drug discovery.

Prof. Subramanya has made significant contributions to the field of macromolecular crystallography, with particular emphasis on proteins involved in human diseases, including cancer and infectious disorders. His research has resulted in 19 patents and 50+ publications in leading peer-reviewed international journals and has been widely cited within the structural biology and drug discovery communities.

Prior to joining Chanakya University, Prof. Subramanya held senior positions at premier research institutes in India, including the Director position in Institute of Bioinformatics and Applied Biotechnology (IBAB), Bengaluru. He has been actively involved in mentoring graduate students and postdoctoral researchers, many of whom have gone on to successful academic and industry careers.

Prof. Subramanya teaches courses in various academic programs of SBS. He has served on several academic committees and review panels and has been a recipient of competitive research grants from national funding agencies. Through his combined efforts in research, teaching, and academic leadership, Prof. Subramanya continues to contribute to advancing molecular biosciences and translational biomedical research in India.

  • Ph.D., 1993, Indian Institute of Science, Bengaluru
  • Postdoctoral Research, 1993-98, University of Oxford, UK

  1. A. H. Arole, P. Deshmukh, A. Sridhar, S. Mathur, M. Mahalingaswamy, H. S. Subramanya, N. D. Nanjaiah, and B. Padmanabhan, “Structural and biochemical insights into purine-based drug molecules in hBRD2 delineate a unique binding mode opening new vistas in the design of inhibitors of the BET family,” Acta Cryst. D, vol. 79, pp. 758–774, 2023.
  2. B. Ambaru, G. M. Gangadharan, H. S. Subramanya, and C. M. Gupta, “Profilin is involved in G1 to S phase progression and mitotic spindle orientation during Leishmania donovani cell division cycle,” PLOS ONE, vol. 17, no. 3, 2022.
  3. R. Poddutoori, K. Aardalen, K. Aithal, S. S. Barahagar, C. Belliappa, M. Bock, S. Chelur, A. Gerken, S. Gopinath, B. Gruenenfelder, M. Kiffe, M. Krishnaswami, J. Langowski, S. Madapa, K. Narayanan, C. Pandit, S. K. Panigrahi, M. Perrone, R. K. Potakamuri, M. Ramachandra, A. Ramanathan, R. Ramos, E. Sager, S. Samajdar, H. S. Subramanya, D. S. Thimmasandra, E. Venetsanakos, and H. Möbitz, “Discovery of MAP855, an efficacious and selective MEK1/2 inhibitor with an ATP-competitive mode of action,” J. Med. Chem., vol. 65, no. 5, pp. 4350–4366, 2022.
  4. S. Nadig, S. Murthy, M. Vandanashree, H. S. Subramanya, B. Gopal, and S. Vembar, “Draft genome sequence of the community-associated Staphylococcus aureus sequence type 88 strain LVP-7, isolated from an ocular infection,” Microbiol. Resour. Announc., vol. 10, no. 7, e00077-21, 2021.
  5. V. Bernard, S. Moudgalya, D. Reegan, P. Sreekanthreddy, A. Mohan, H. S. Subramanya, S. S. Vembar, and S. Ghosh, “Whole genome sequences of Aedes aegypti (Linn.) field isolates from Southern India,” bioRxiv, 2020.
  6. B. Ambaru, A. Gopalsamy, T. V. S. Tammana, H. S. Subramanya, and C. M. Gupta, “Actin sequestering protein, profilin, regulates intracellular vesicle transport in Leishmania,” Mol. Biochem. Parasitol., vol. 238, p. 111280, 2020.
  7. S. Kumari and H. S. Subramanya, “Network pharmacology study of Curcuma longa L.: potential target proteins and their functional enrichment analysis,” BMC Res. Notes, vol. 13, no. 1, pp. 1–5, 2020.
  8. G. McDonald, V. Chubukov, J. Coco, K. Truskowski, R. Narayanaswamy, S. Choe, M. Steadman, E. Artin, A. K. Padyana, L. Jin, S. Ronseaux, C. Locuson, Z.-P. Fan, T. Erdmann, A. Mann, S. Hayes, M. Fletcher, K. Nellore, S. S. Rao, H. S. Subramanya, K. S. Reddy, S. K. Panigrahi, T. Antony, S. Gopinath, Z. Sui, N. N. Nagaraja, L. Dang, G. Lenz, J. Hurov, S. A. Biller, J. Murtie, K. M. Marks, and D. B. Ulanet, “Selective vulnerability to pyrimidine starvation in hematologic malignancies revealed by AG-636, a novel clinical-stage inhibitor of dihydroorotate dehydrogenase,” Mol. Cancer Ther., vol. 19, no. 12, pp. 2502–2515, 2020.
  9. V. R. Gummadi, A. Boruah, B. R. Ainan, B. R. Vare, S. Manda, H. P. Gondle, S. N. Kumar, S. Mukherjee, S. T. Gore, N. R. Krishnamurthy, S. Marappan, S. S. Nayak, K. Nellore, W. R. Balasubramanian, A. Bhumireddy, S. Giri, S. S. Gopinath, D. S. Samiulla, G. Daginakatte, A. Basavaraju, S. Chelur, R. Eswarappa, C. Belliappa, H. S. Subramanya, R. N. Booher, M. Ramachandra, and S. Samajdar, “Discovery of CA-4948, an orally bioavailable IRAK4 inhibitor for treatment of hematologic malignancies,” ACS Med. Chem. Lett., vol. 11, no. 12, pp. 2374–2381, 2020.
  10. H. S. Subramanya and G. Saberwal, “India needs more policy research,” Curr. Sci., vol. 116, no. 8, pp. 1279–1280, 2019.
  11. N. Chaturvedi, B. Mehrotra, S. Kumari, S. Gupta, H. S. Subramanya, and G. Saberwal, “Some data quality issues at Clinical Trials,” Trials, vol. 20, p. 378, 2019.
  12. A. K. M. Fairus, B. Choudhary, S. Hosahalli, N. Kavitha, and O. Shatrah, “Dihydroorotate dehydrogenase (DHODH) inhibitors affect ATP depletion, endogenous ROS and mediate S-phase arrest in breast cancer cells,” Biochimie, vol. 135, pp. 154–163, 2017.
  13. M. S. Dorasamy, B. Choudhary, K. Nellore, H. Subramanya, and P. F. Wong, “Dihydroorotate dehydrogenase inhibitors target c-Myc and arrest melanoma, myeloma and lymphoma cells at S-phase,” J. Cancer, vol. 8, no. 15, pp. 3086–3098, 2017.
  14. I. Abdullah, C. F. Chee, Y.-K. Lee, S. S. R. Thunuguntla, K. S. Reddy, K. Nellore, T. Antony, J. Verma, K. W. Mun, O. Shatrah, H. Subramanya, and N. A. Rahman, “Benzimidazole derivatives as potential dual inhibitors for PARP-1 and DHODH,” Bioorg. Med. Chem., vol. 23, no. 15, pp. 4669–4680, 2015.
  15. K. Narasimha Rao, A. Lakshminarasimhan, S. Joseph, S. U. Lekshmi, M.-S. Lau, M. Takhi, K. Sreenivas, S. Nathan, R. Yusof, N. A. Rahman, M. Ramachandra, T. Antony, and H. Subramanya, “AFN-1252 is a potent inhibitor of enoyl-ACP reductase from Burkholderia pseudomallei: Crystal structure, mode of action, and biological activity,” Protein Sci., vol. 24, pp. 832–840, 2015.
  16. R. Goswami, G. Wohlfahrt, S. Mukherjee, C. Ghadiyaram, J. Nagaraj, L. K. Satyam, K. Subbarao, S. Gopinath, N. R. Krishnamurthy, H. S. Subramanya, and M. Ramachandra, “Discovery of O-(3-carbamimidoylphenyl)-l-serine amides as matriptase inhibitors using a fragment-linking approach,” Bioorg. Med. Chem. Lett., vol. 25, no. 3, pp. 616–620, 2015.
  17. M. V. V. V. Sekhar Reddy, C. Ghadiyaram, S. K. Panigrahi, N. R. Krishnamurthy, H. S. Subramanya, A. P. Chandrasekharappa, D. Manna, S. E. Badiger, P. K. Dubey, and L. N. Mangamoori, “X-ray structure of PTP1B in complex with a new PTP1B inhibitor,” Protein Pept. Lett., vol. 21, no. 1, pp. 90–93, 2014.
  18. M. Takhi, K. Sreenivas, C. K. Reddy, M. Munikumar, K. Praveena, P. Sudheer, B. N. V. M. Rao, G. Ramakanth, J. Sivaranjani, S. Mulik, Y. R. Reddy, K. N. Rao, R. Pallavi, A. Lakshminarasimhan, S. K. Panigrahi, T. Antony, I. Abdullah, Y.-K. Lee, M. Ramachandra, R. Yusof, N. A. Rahman, H. Subramanya, “Discovery of azetidine based ene-amides as potent bacterial enoyl ACP reductase (FabI) inhibitor,” Eur. J. Med. Chem., vol. 84, pp. 382–394, 2014.
  19. V. Basetti, R. Pallepati, S. H. Subramanya, and V. Potluri, “A facile synthesis of 7,12-dihydro-1,3,6,7,12-pentaazapleiadenes by domino reaction,” Heterocycl. Commun., vol. 20, no. 4, pp. 207–214, 2014.
  20. R. Goswami, S. Mukherjee, C. Ghadiyaram, G. Wohlfahrt, R. K. Sistla, J. Nagaraj, L. K. Satyam, K. Subbarao, R. K. Palakurthy, S. Gopinath, N. R. Krishnamurthy, T. Ikonen, A. Moilanen, H. S. Subramanya, P. Kallio, and M. Ramachandra, “Structure-guided discovery of 1,3,5 tri-substituted benzenes as potent and selective matriptase inhibitors exhibiting in vivo antitumor efficacy,” Bioorg. Med. Chem., vol. 22, no. 12, pp. 3187–3203, 2014.
  21. R. Goswami, S. Mukherjee, G. Wohlfahrt, C. Ghadiyaram, J. Nagaraj, B. R. Chandra, R. K. Sistla, L. K. Satyam, D. S. Samiulla, A. Moilanen, H. S. Subramanya, and M. Ramachandra, “Discovery of Pyridyl Bis(oxy)dibenzimidamide Derivatives as Selective Matriptase Inhibitors,” ACS Med. Chem. Lett., vol. 4, no. 12, pp. 1152–1157, 2013.
  22. M. V. Reddy, C. Ghadiyaram, S. K. Panigrahi, H. S. Subramanya, and L. N. Mangamoori, “Diphenylether derivative as selective inhibitor of protein tyrosine phosphatase 1B (PTP1B) over t-cell protein tyrosine phosphatase (TCPTP) identified through virtual screening,” Mini Rev. Med. Chem., vol. 13, no. 11, pp. 1602–1606, 2013.
  23. V. R. Gummadi, S. Rajagopalan, L. C. Yeng, M. Paydar, G. A. Renukappa, B. R. Ainan, N. R. Krishnamurthy, S. K. Panigrahi, K. Mahasweta, S. Raghuramachandran, M. Rajappa, A. Ramanathan, A. Lakshminarasimhan, M. Ramachandra, W. P. Fong, M. R. Mustafa, S. Nanduri, H.S. Subramanya, “Discovery of 7-azaindole based anaplastic lymphoma kinase (ALK) inhibitors: Wild type and mutant (L1196M) active compounds with unique binding mode,” Bioorg. Med. Chem. Lett., vol. 23, no. 17, pp. 4911–4918, 2013.
  24. V. Basetti, R. Pallepati, H. S. Subramanya, and V. Potluri, “A facile synthesis of tetracyclic benzo-pyridonaphthyridines by domino reaction,” Tetrahedron Lett., vol. 54, no. 15, pp. 2014–2017, 2013.
  25. R. S., C. G., C. S. Nagaraja, and H. S. Subramanya, “A structure-based strategy for new drug discovery,” IPT, vol. 20, pp. 18, 2006.
  26. S. Bhavani, V. Trivedi, M. Ambili, J. V. R. Jala, H. S. Subramanya, K. Purnima, V. Prakash, N. Appaji Rao, and H. S. Savithri, “Role of Lys-226 in the catalytic mechanism of Bacillus stearothermophilus serine hydroxymethyltransferase – Crystal structure and kinetic studies,” Biochemistry, vol. 44, pp. 6929–6937, 2005.
  27. U. Varshney, V. Ramesh, A. Madabushi, R. Gaur, H. S. Subramanya, and U. L. RajBhandary, “Mycobacterium tuberculosis Rv2118c codes for a single-component homotetrameric m1A58 tRNA methyltransferase,” Nucleic Acids Res., vol. 32, pp. 1018–1027, 2004.
  28. N. Appaji Rao, M. Ambili, J. V. R. Jala, H. S. Subramanya, and H. S. Savithri, “Structure-function relationship in serine hydroxymethyltransferase,” Biochim. Biophys. Acta, vol. 1647, pp. 24–29, 2003.
  29. A. N. Bhatt, K. Prakash, H. S. Subramanya, and V. Bhakuni, “Different unfolding pathways for mesophilic and thermophilic homologues of serine hydroxymethyltransferase,” Biochemistry, vol. 41, pp. 12115–12123, 2002.
  30. V. Trivedi, A. Gupta, J. V. K. Rao, P. Saravanan, G. S. J. Rao, A. N. Rao, H. S. Savithri, and H. S. Subramanya, “Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from B. stearothermophilus: Insights into the catalytic mechanism,” J. Biol. Chem., vol. 277, pp. 17161–17169, 2002.
  31. B. Datta, P. Chakrabarti, H. S. Subramanya, and P. Parrack, “Purification and crystallization of CII: An unstable transcription activator from phage lambda,” Biochem. Biophys. Res. Commun., vol. 288, pp. 997–1000, 2001.
  32. A. Gupta, P. H. Kumar, T. K. Dineshkumar, U. Varshney, and H. S. Subramanya, “Crystal structure of Rv2118c: An AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv,” J. Mol. Biol., vol. 312, pp. 381–391, 2001.
  33. S. Sarkhel, G. K. Jain, S. Singh, H. S. Subramanya, and P. R. Maulik, “Dysobinin, a tetranortriterpenoid,” Acta Crystallogr. C, vol. 56, pp. E253–E254, 2000.
  34. G. R. Desiraju, B. Gopalakrishnan, R. K. R. Jetti, D. Raveendra, J. A. R. P. Sarma, and H. S. Subramanya, “Three-dimensional quantitative structural activity relationship (3D-QSAR) studies of some 1,5-diarylpyrazoles: Analogue based design of selective cyclooxygenase-2 inhibitors,” Molecules, vol. 5, pp. 945–955, 2000.
  35. S. S. Velankar, P. Soultanas, M. S. Dillingham, H. S. Subramanya, and D. B. Wigley, “Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism,” Cell, vol. 97, pp. 75–84, 1999.
  36. L. E. Bird, J. A. Brannigan, H. S. Subramanya, and D. B. Wigley, “Characterization of Bacillus stearothermophilus PcrA helicase: Evidence against an active rolling model,” Nucleic Acids Res., vol. 26, pp. 2686–2693, 1998.
  37. L. E. Bird, H. S. Subramanya, and D. B. Wigley, “Helicases: A unifying structural theme?” Curr. Opin. Struct. Biol., vol. 8, pp. 14–18, 1998.
  38. H. S. Subramanya, L. K. Arciszewska, R. Baker, L. E. Bird, D. J. Sherrat, and D. B. Wigley, “Crystal structure of the site specific recombinase XerD,” EMBO J., vol. 16, pp. 5178–5187, 1997.
  39. M. R. N. Murthy, M. Bhuvaneswari, H. S. Subramanya, K. Gopinath, and H. S. Savithri, “Structure of sesbania mosaic viruses at 3 Å resolution,” Biophys. Chem., vol. 68, pp. 33–42, 1997.
  40. M. Bhuvaneswari, H. S. Subramanya, M. R. N. Murthy, K. Gopinath, and H. S. Savithri, “Architecture of small RNA viruses,” Prog. Crystal Growth Charact., vol. 34, pp. 1–10, 1997.
  41. F. T. F. Tsai, H. S. Subramanya, J. A. Brannigan, and D. B. Wigley, “Crystallization and preliminary crystallographic analysis of the DNA gyrase B protein from B. stearothermophilus,” Acta Cryst., pp. 1216–1218, 1996.
  42. H. S. Subramanya, L. E. Bird, J. A. Brannigan, and D. B. Wigley, “Crystal structure of a Dexx box DNA helicase,” Nature, vol. 384, pp. 379–383, 1996.
  43. H. S. Subramanya, A. J. Doherty, S. R. Ashford, and D. B. Wigley, “Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7,” Cell, vol. 85, no. 4, pp. 607–615, 1996.
  44. A. J. Doherty, S. R. Ashford, H. S. Subramanya, and D. B. Wigley, “Bacteriophage T7 DNA ligase: Overexpression, purification, crystallization and characterization,” J. Biol. Chem., vol. 271, pp. 11083–11089, 1996.
  45. H. S. Subramanya, H. Peng, K. J. Marians, and D. B. Wigley, “Preliminary crystallographic analysis of the ParE subunit of E. coli topoisomerase IV,” Acta Cryst., vol. D52, pp. 579–580, 1996.
  46. H. S. Subramanya, D. I. Roper, Z. Dauter, E. J. Dodson, G. J. Davis, K. S. Wilson, and D. B. Wigley, “Enzymatic ketonization of 2-hydroxymuconate: Specificity and mechanism investigated by the crystal structure of two isomerases,” Biochemistry, vol. 35, pp. 792–802, 1996.
  47. M. Bhuvaneswari, H. S. Subramanya, K. Gopinath, H. S. Savithri, M. V. Nayudu, and M. R. N. Murthy, “Structure of sesbania mosaic virus at 3 Å resolution,” Structure, vol. 3, no. 10, pp. 1021–1030, 1995.
  48. H. S. Subramanya, “Structure of sesbania mosaic virus at 4.7 Å resolution,” J. Indian Inst. Sci., vol. 75, pp. 720–722, 1995.
  49. D. I. Roper, H. S. Subramanya, V. Shingler, and D. B. Wigley, “Preliminary crystallographic analysis of 4-oxalocrotonate tautomerase reveals the oligomeric structure of the enzyme,” J. Mol. Biol., vol. 243, pp. 799–801, 1994.
  50. H. S. Subramanya, K. Gopinath, M. V. Nayudu, H. S. Savithri, and M. R. N. Murthy, “Structure of sesbania mosaic virus at 4.7 Å resolution and partial sequence of the coat protein,” J. Mol. Biol., vol. 229, pp. 20–25, 1993.

Patents

  1. Azine Compounds as Glucokinase Activators (2009) SE Badiger, KF Fosgerau, N Vrang, VD Chaudhari, JJ Naik, J Auxcilia, RR Reddy, HS Subramanya, PV Reddy, BNS Reddy, WO2009/083553A1
  2. Hetereocyclic Compounds as MEK Inhibitors (2010) D Chikkanna, C McCarthy, H Moebitz, C Pandit, R Sistla, H Subramanya WO/2010/121646
  3. Piperazine derivatives as inhibitors of stearoyl-CoA desaturase (2011) K Sundaresan, SN Raikar, SR Sammeta, G Prabhu, H Subramanya, A Bischoff US Patent 8,039,463
  4. Piperidine derivatives as inhibitors of stearoyl-CoA desaturase (2012) K Sundaresan, PBK Rao, B Ainan, H Ayyamperumal, AR Girish, S Tatiparthy, G Prabhu, H Subramanya, A Bischoff US Patent 8,129,376
  5. Substituted quinazoline and pyrido-pyrimidine derivatives (2012) RA Smith, SK Thompson, S Hosahalli, M Bejugam, S Nanduri, P Sunil Kumar, M Natarajan WO/2012/058671
  6. Isoxazolines as therapeutic agents (2012) DJ Calderwood, EC Breinlinger, SL Swann, VS Chitty, S Hosahalli WO/2012/151158
  7. Substituted pyridine derivatives as FABI inhibitors (2013) M Takhi, S Hosahalli, SK Panigrahi, MK Mahadari, CR Kottam, N Abd Rahman, R Yusof WO/2013/080222
  8. Bicyclic Heterocycles as IRAK4 Inhibitors (2013) A Boruah, HS Subramanya, S Mukherjee WO/2013/042137
  9. Trisubstituted Benzotriazole Derivatives as Dihydroorotate Oxygenase Inhibitors (2014) SSR Thunuguntla, S Hosahalli, SR Kunnam WO/2014/128669
  10. Tetrahydropyridine derivatives as FabI inhibitors (2015) M Takhi, S Hosahalli, SK Panigrahi WO/2014/195844
  11. Dihydroorotate Dehydrogenase Inhibitors (2015) SSR Thunuguntla, H Subramanya, SR Kunnam, SRS Vijay, C Bingi, R Kusanur, M Schwarz, M Arlt US9006454B2
  12. Bicyclic heterocycle derivatives as bromodomain inhibitors (2015) S Samajdar, C Abbineni, S Sasmal, S Hosahalli WO2015104653A1
  13. Substituted amino-pyrimidine derivatives (2015) RA Smith, A Venkatesan, M Bejugam, S Hosahalli, S Nanduri US 9145411B2
  14. 3-(pyrazolyl)-1H-pyrrolo [2, 3-b] pyridine derivatives as kinase inhibitors (2016) VR Gummadi, S Hosahalli, S Nanduri, GA Renukappa US Patent 9,353,107
  15. Crystalline Structure of FABI from Burkholderia Pseudomallei (2017) NR Krishnamurthy, A Lakshminarasimhan, T Antony, HS Subramanya US20170088822A1
  16. Quinazolines and azaquinazolines as dual inhibitors of RAS/RAF/MEK/ERK and PI3K/AKT/PTEN/mTOR pathways SK Thompson, RA Smith, S Reddy, TM John, VK Nyavanandi, S Hosahalli, V Potluri, SK Panigrahi, PR Nadipalli, S Sengupta (2019) US Patent 10,226,468
  17. Pyrimido-pyridazinone compounds and methods of use thereof (2019) A Venkatesan, RA Smith, H Subramanya, V Potluri, SK Panigrahi, V Basetti, K Kunta US Patent 10,183,944
  18. 1, 4, 6-trisubstituted-2-alkyl-1H-benzo [d] imidazole derivatives as dihydroorotate oxygenase inhibitors (2020) SSR Thunuguntla, S Hosahalli, SK Panigrahi, M Schwarz, M Arlt (2020) WO2018154088A1
  19. Methods of use for trisubstituted benzotriazole derivatives as dihydroorotate oxygenase inhibitors (2021) K Nellore, S Hosahalli WO2018197997A1

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