M. Vijayan

Mamannamana Vijayan
Born 16 Oct 1941
Cherpu, Kerala
Residence Bangalore
Nationality Indian
Fields Biological sciences
Institutions Indian Institute of Science
Alma mater Indian Institute of Science
Doctoral advisor M. A. Viswamitra
Known for Protein crystallography
Notable awards Padma Shri (2004), Shanti Swarup Bhatnagar Prize for Science and Technology(1985)

Mamannamana Vijayan (born 16 October 1941, Cherpu, Kerala[1]) is an Indian structural biologist. His main area of research is protein structures. His contributions have been towards the structure and carbohydrate specificity of lectins and protein hydration. He has also contributed towards the area of structure and interactions of mycobacterial proteins and supramolecular association with reference to chemical evolution and origin of life. Vijayan did biological macromolecular crystallography in India.[1]

He was awarded Padma Shri by the President of India in 2004.[2] He was the President of the Indian National Science Academy from 2007–2010.[3] Currently, he is DAE Homi Bhabha Professor at the Indian Institute of Science.

Education

Vijayan obtained his Masters of Science degree in 1963 from Allahabad University. Thereafter, he received his Doctorate degree in X-ray crystallography from the Indian Institute of Science in 1967. During 1968–71, he was a post-doctoral fellow in Professor Dorothy Hodgkin’s research group at University of Oxford. During that period, he studied x-ray diffraction data for insulin crystals.[4]

Contribution in structural biology

Vijayan's students and postdocs have dealt with four of the five structural classes of plant lectins. They have studied in detail lectins from peanut, winged bean (basic and acidic), jackfruit (jacalin and artocarpin), garlic, banana and snake gourd. The work on lectins demonstrated the need for considering open quaternary structures when dealing with multimeric proteins[5] and the variability in the quaternary association of legume lectins.[6][7][8] and lectins with the β-prism I fold.[9] His group established β-prism I fold as a lectin fold.[10] They explained the roles of water-bridges, post-translational modification, oligomerisation and variation in loop length as strategies for generating ligand specificity.[11][12][13][14][15][16] Their studies provided insights into the structural basis of carbohydrate specificity and the biological implications of this specificity.[17][18][19][20][21][22] Using an approach involving water-mediated transformations, Vijayan's research determined the nature of the flexibility in lysozyme and ribonuclease A and identified the invariant features in their hydration shells.[23][24][25] His research also demonstrated the presence of ensembles of relaxed and tense states of haemoglobin.[26] and water-mediated loop movement in β-lactoglobulin.[27] His studies have provided insights into the relationship among hydration, molecular mobility and protein action.

Vijayan organised a national programme on the structural biology of microbial pathogens. His research in the area has been concerned with mycobacterial, particularly tuberculosis, related proteins. The specific systems studied by him include RecA, RuvA, uracil DNA glycosylase, single stranded DNA binding protein, ribosome recycling factor, peptidyl tRNA hydrolase, pantothenate kinase and DNA binding protein in stationary phase cells.[28][29][30][31][32][33][34][35][36][37] He has elucidated the specific structural features of these proteins in mycobacteria, which, among other things, have opened up avenues for structure-based inhibitor design, with the eventual objective of drug development.

Vijayan's research have determined the molecular recognition and aggregation patterns involving amino acids and peptides using an approach based on molecular complexes. This has implications to chemical evolution and origins of life.[38][39] His other contributions pertain to the structure and interactions of non-steroidal anti-inflammatory analgesics,[40] ionophores and related compounds,[41] side chain conformation in proteins[42] and additional binding sites in lysozyme.[43]

Vijayan has published more than 260 peer reviewed research articles and has guided 38 research students and 20 postdoctoral fellows.[1]

Professional life

After completing his postdoctoral research at the University of Oxford, he returned to India in 1971 and joined the Molecular Biophyiscs Unit at the Indian Institute of Science (IISc). He has served in various capacities such as Professor, Chairman of Molecular Biophysics Unit, Chairman of Division of Biological Sciences among others. During 2000–2004 he was Associate Director of IISc.[1] He has continued to work at the Institute as a DBT Distinguished Biotechnologist and subsequently as a DAE Homi Bhabha Professor.

Role in international and national organisations

Vijayan is a member of the International Union of Crystallography (IUCr), the International Union of Pure & Applied Biophysics (IUPAB), the International Council for Science (ICSU), the Inter Academy Panel (IAP) and the InterAcademy Council (IAC). He is a former President of the Asian Crystallographic Association.[1] He has been involved in the activities of the science departments and agencies of the Government of India and different scientific institutions in the country. He is the Founder President of the Indian Crystallographic Association[44] and has served as the President of the Indian Biophysical Society and the President of the Indian National Science Academy (2007–2010).[3]

Awards and recognitions

Vijayan is a Fellow of the three science academies of India[1] and the Academy of Sciences for the Developing World (TWAS).[45] He has won the Shanti Swarup Bhatnagar Prize, GN Ramachandran Medal by INSA, Alumni Award Excell. Res. by IISc, FICCI Award Life Sci., Ranbaxy Res. Award by Basic Medical Sciences, JL Nehru Centen. vis. fellow by INSA, Om Prakash Bhasin Award, KS Krishnan Memorial Lecture by INSA, JL Nehru Birth Centen. Award by Indian Science Congress Assoc., Padma Shri,[2] Distinguished Biotechnologist Award by DBT; Goyal Prize, first CSIR/Science Congress GN Ramachandran Award for Excellence in Biological Science and Technology, Distinguished Alumni Award and Lakshmipat Singhania-IIM Lucknow National Leadership Award for Science and Technology-Leader, 2009.

References

  1. 1 2 3 4 5 6 "About M. Vijayan". InterAcademy Council. 2003. Retrieved 20 September 2010.
  2. 1 2 "Padma Shri Awardees". Government of India. 2005. Retrieved 2010-09-12.
  3. 1 2 "About INSA: Advisory Committees for the Year 2010". India National Science Society. Retrieved 20 September 2010.
  4. ↑ Adams, M.J.; Blundell, T.L.; Dodson, E.J.; Dodson, G.G.; Vijayan, M.; Baker, E.N.; Harding, M.M.; Hodgkin, D.C.; et al. (1 November 1969). "Structure of Rhombohedral 2 Zinc Insulin Crystals" (PDF). Nature 224 (5218): 491–495. Bibcode:1969Natur.224..491A. doi:10.1038/224491a0. Retrieved 20 September 2010.
  5. ↑ Banerjee, R.; Mande, S.C.; Ganesh, V.; Das, K.; Dhanaraj, V.; Mahanta, S.K.; Suguna, K.; Surolia, A.; Vijayan, M. (4 January 1994). "Crystal structure of peanut lectin, a protein with an unusual quaternary structure". Proceedings of the National Academy of Sciences 91 (1): 227–231. Bibcode:1994PNAS...91..227B. doi:10.1073/pnas.91.1.227. PMC 42920. PMID 8278370. Retrieved 20 September 2010.
  6. ↑ Prabu, M.M.; Sankaranarayanan, R.; Puri, K.D.; Sharma, V.; Surolia, A.; Vijayan, M.; Suguna, K. (6 March 1998). "Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution". Journal of Molecular Biology 276 (4): 787–96. doi:10.1006/jmbi.1997.1568. PMID 9500920.
  7. ↑ Prabu, M.M.; Suguna, K.; Vijayan, M. (1 April 1999). "Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins". Proteins 35 (1): 58–69. doi:10.1002/(SICI)1097-0134(19990401)35:1<58::AID-PROT6>3.0.CO;2-A. PMID 10090286.
  8. ↑ Kulkarni, K.A.; Srivastava, A.; Mitra, N.; Sharon, N.; Surolia, A.; Vijayan, M.; Suguna, K. (1 September 2004). "Effect of glycosylation on the structure of Erythrina corallodendron lectin". Proteins 56 (4): 821–7. doi:10.1002/prot.20168. PMID 15281133.
  9. ↑ Singh, D.D.; Saikrishnan, K.; Kumar, P.; Surolia, A.; Sekar, K.; Vijayan, M. (October 2005). "Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies". Glycobiology 15 (10): 1025–32. doi:10.1093/glycob/cwi087. PMID 15958419.
  10. ↑ Sankaranarayanan, R.; Sekar, K.; Banerjee, R.; Sharma, V.; Surolia, A.; Vijayan, M. (July 1996). "A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold". Nature Structural Biology 3 (7): 596–603. doi:10.1038/nsb0796-596. PMID 8673603.
  11. ↑ Ravishankar, R.; Ravindran, M.; Suguna, K.; Surolia, A.; Vijayan, Vijayan (10 June 1997). "Crystal structure of the peanut lectin – T-antigen complex. Carbohydrate specificity generated by water bridges". Current Science 72 (11). Retrieved 20 September 2010.
  12. ↑ Arockia Jeyaprakash, A.; Jayashree, G.; Mahanta, S.K.; Swaminathan, C.P.; Sekar, K.; Surolia, A.; Vijayan, M. (18 March 2005). "Structural basis for the energetics of jacalin-sugar interactions: promiscuity versus specificity". Journal of Molecular Biology 347 (1): 181–188. doi:10.1016/j.jmb.2005.01.015. PMID 15733927.
  13. ↑ Chandra, N.R.; Ramachandraiah, G.; Bachhawat, K.; Dam, T.K.; Surolia, A.; Vijayan, M. (22 January 1999). "Crystal structure of a dimeric mannose-specific agglutinin from garlic: Quaternary association and carbohydrate specificity". Journal of Molecular Biology 285 (3): 1157–68. doi:10.1006/jmbi.1998.2353. PMID 9887270.
  14. ↑ Manoj, N.; Srinivas, V.R.; Surolia, A.; Vijayan, M.; Suguna, K. (6 October 2000). "Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin". Journal of Molecular Biology 302 (5): 1129–37. doi:10.1006/jmbi.2000.4111. PMID 11183779.
  15. ↑ Jeyaprakash, A.A.; Srivastav, A.; Surolia, A.; Vijayan, M. (7 May 2004). "Structural basis for the carbohydrate specificities of artocarpin: Variation in the length of a loop as a strategy for generating ligand specificity". Journal of Molecular Biology 338 (4): 757–770. doi:10.1016/j.jmb.2004.03.040. PMID 15099743.
  16. ↑ Vijayan, M.; Chandra, N. (9 December 1999). "Lectins". Current Opinion in Structural Biology 9 (6): 707–714. doi:10.1016/S0959-440X(99)00034-2. PMID 10607664.
  17. ↑ Banerjee, R.; Das, K.; Ravishankar, R.; Suguna, K.; Surolia, A.; Vijayan, M. (7 June 1996). "Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex". Journal of Molecular Biology 259 (2): 281–296. doi:10.1006/jmbi.1996.0319. PMID 8656429.
  18. ↑ Pratap, J.V.; Jeyaprakash, A.A.; Rani, P.G.; Sekar, K.; Surolia, A.; Vijayan, M. (22 March 2001). "Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-D-mannose: implications to the generation of carbohydrate specificity". Journal of Molecular Biology 317 (2): 237–247. doi:10.1006/jmbi.2001.5432. PMID 11902840.
  19. ↑ Ramachandraiah, G.; Chandra, N.R.; Surolia, A.; Vijayan, M. (November 2003 Nov). "Computational analysis of multivalency in lectins: Structures of garlic lectin-oligosaccharide complexes and their aggregates". Glycobiology 13 (11): 765–75. doi:10.1093/glycob/cwg095. PMID 12851290. Check date values in: |date= (help)
  20. ↑ Kulkarni, K.A.; Katiyar, S.; Surolia, A.; Vijayan, M.; Suguna, K. (15 August 2007). "Generation of blood group specificity: New insights from structural studies on the complexes of A- and B-reactive saccharides with basic winged bean agglutinin". Proteins 68 (3): 762–769. doi:10.1002/prot.21428. PMID 17510954.
  21. ↑ Kundhavai Natchiar, S.; Suguna, K.; Surolia, A.; Vijayah, M. (2007). "Peanut agglutinin, a lectin with an unusual quaternary structure and interesting ligand binding properties". Crystallographic Reviews (13): 1–26.
  22. ↑ Sharma, A.; Sekar, K.; Vijayan, M. (December 2009). "Structure, dynamics, and interactions of jacalin. Insights from molecular dynamics simulations examined in conjunction with results of X-ray studies". Proteins 77 (4): 760–77. doi:10.1002/prot.22486. PMID 19544573.
  23. ↑ Kodandapani, R.; Suresh, C.G.; Vijayan, M. (25 September 1990). "Crystal structure of low humidity tetragonal lysozyme at 2.1-A resolution. Variability in hydration shell and its structural consequences". Journal of Biological Chemistry 265 (27): 16126–16131. PMID 2398048.
  24. ↑ Kishan, R.V.; Chandra, N.R.; Sudarsanakumar, C.; Suguna, K.; Vijayan, M. (1 September 1995). "Water-dependent domain motion and flexibility in ribonuclease A and the invariant features in its hydration shell. An X-ray study of two low-humidity crystal forms of the enzyme". Acta Crystallographica D 51 (Pt 5): 703–10. doi:10.1107/S0907444994014794. PMID 15299799.
  25. ↑ Nagendra, H.G.; Sukumar, N.; Vijayan, M. (1 August 1998). "=Role of water in plasticity, stability, and action of proteins: The crystal structures of lysozyme at very low levels of hydration". Proteins 32 (2): 229–240. doi:10.1002/(SICI)1097-0134(19980801)32:2<229::AID-PROT9>3.0.CO;2-F. PMID 9714162.
  26. ↑ Sankaranarayanan, R.; Biswal, B.K.; Vijayan, M. (15 August 2005). "A new relaxed state in horse methemoglobin characterized by crystallographic studies". Proteins 60 (3): 547–51. doi:10.1002/prot.20510. PMID 15887226.
  27. ↑ Vijayalakshmi, L.; Krishna, R.; Sankaranarayanan, R.; Vijayan, M. (April 2008). "An asymmetric dimer of beta-lactoglobulin in a low humidity crystal form – structural changes that accompany partial dehydration and protein action". Proteins 71 (1): 241–249. doi:10.1002/prot.21695. PMID 17932936.
  28. ↑ Datta, S.; Prabu, M.M.; Vaze, M.B.; Ganesh, N.; Chandra, N.R.; Muniyappa, K.; Vijayan, S. (15 December 2000). "Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): Implications for decreased ATPase activity and molecular aggregation". Nucleic Acids Research 28 (24): 4964–4973. doi:10.1093/nar/28.24.4964. PMC 115232. PMID 11121488.
  29. ↑ Saikrishnan, K.; Jeyakanthan, J.; Venkatesh, J.; Acharya, N.; Sekar, K.; Varshney, U.; Vijayan, M. (8 August 2003). "Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications". Journal of Molecular Biology 331 (2): 385–93. doi:10.1016/S0022-2836(03)00729-0. PMID 12888346.
  30. ↑ Saikrishnan, K.; Kalapala, S.K.; Varshney, U.; Vijayan, M. (7 January 2005). "X-ray structural studies of Mycobacterium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications". Journal of Molecular Biology 345 (1): 29–38. doi:10.1016/j.jmb.2004.10.034. PMID 15567408.
  31. ↑ Vijayan, M. (2005). "Structural biology of mycobacterial proteins: The Bangalore effort". Tuberculosis 85 (5–6): 357–366. doi:10.1016/j.tube.2005.08.011. PMID 16260182.
  32. ↑ Krishna, R.; Prabu, J.R.; Manjunath, G.P.; Datta, S.; Chandra, N.R.; Muniyappa, K.; Vijayan, M. (6 April 2007). "Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobacterium smegmatis RecA". Journal of Molecular Biology 367 (4): 1130–1144. doi:10.1016/j.jmb.2007.01.058. PMID 17306300.
  33. ↑ Selvaraj, M.; Roy, S.; Singh, N.S.; Sangeetha, R.; Varshney, U.; Vijayan, M. (7 September 2007). "Structural plasticity and enzyme action: crystal structures of mycobacterium tuberculosis peptidyl-tRNA hydrolase". Journal of Molecular Biology 372 (1): 186–93. doi:10.1016/j.jmb.2007.06.053. PMID 17619020.
  34. ↑ Roy, S.; Saraswathi, R.; Chatterji, D.; Vijayan, M. (25 January 2008). "Structural studies on the second Mycobacterium smegmatis Dps: Invariant and variable features of structure, assembly and function". Journal of Molecular Biology 375 (4): 948–959. doi:10.1016/j.jmb.2007.10.023. PMID 18061613.
  35. ↑ Kaushal, P.S.; Talawar, R.K.; Krishna, P.D.; Varshney, U.; Vijayan, M. (May 2008). "Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: Structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources". Acta Crystallographica D 64 (Pt 5): 551–560. doi:10.1107/S090744490800512X. PMID 18453691.
  36. ↑ Prabu, J.R.; Thamotharan, S.; Khanduja, J.S.; Chandra, N.R.; Muniyappa, K.; Vijayan, M. (July 2009). "Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA: Additional role of RuvB-binding domain and inter species variability". Biochimica et Biophysica Acta 1794 (7): 1001–1009. doi:10.1016/j.bbapap.2009.04.003. PMID 19374958.
  37. ↑ Chetnani, B.; Kumar, P.; Surolia, A.; Vijayan, M. (9 July 2010). "M. tuberculosis pantothenate kinase: Dual substrate specificity and unusual changes in ligand locations". Journal of Molecular Biology 400 (2): 171–185. doi:10.1016/j.jmb.2010.04.064. PMID 20451532.
  38. ↑ Vijayan, M. (1988). "Molecular interactions and aggregation involving amino acids and peptides and their role in chemical evolution". Progress in Biophysics and Molecular Biology 52 (2): 71–99. doi:10.1016/0079-6107(88)90003-X. PMID 3076685.
  39. ↑ Selvaraj, M.; Thamotharan, S.; Roy, S.; Vijayan, M. (June 2007). "X-ray studies of crystalline complexes involving amino acids and peptides. XLIV. Invariant features of supramolecular association and chiral effects in the complexes of arginine and lysine with tartaric acid". Acta Crystallographica B 63 (Pt 3): 459–68. doi:10.1107/S010876810701107X. PMID 17507759.
  40. ↑ Singh, Tej Pal; Vijayan, Mamannamana (1977). "Structural studies of analgesics and their interactions. Part 4. Crystal structures of phenylbutazone and a 2 : 1 complex between phenylbutazone and piperazine". Journal of the Chemical Society, Perkin Transactions 2 2 (5): 693–699. doi:10.1039/P29770000693.
  41. ↑ Devarajan, S.; Nair, C.M.K.; Easwaran, K.R.K.; Vijayan, M. (7 August 1980). "A novel conformation of valinomycin in its barium complex" (PDF). Nature 286 (5773): 640–641. Bibcode:1980Natur.286..640D. doi:10.1038/286640a0. PMID 7402346.
  42. ↑ Bhat, T.N.; Sasisekharan, V.; Vijayan, M. (February 1979). "An analysis of side-chain conformation in proteins". International Journal of Peptide and Protein Research 13 (2): 170–84. PMID 429093.]
  43. ↑ Madhusudan; Vijayan, M. (July 1992). "Additional binding sites in lysozyme. X-ray analysis of lysozyme complexes with bromophenol red and bromophenol blue". Protein Engineering 5 (5): 399–404. doi:10.1093/protein/5.5.399. PMID 1518787.
  44. ↑ "Past Office Bearers – Year (2001–2003)". Indian Crystallographic Association. Retrieved 20 September 2010.
  45. ↑ "Members: Structural, Cell and Molecular Biology". TWAS. Retrieved 20 September 2010.

External links

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