5WVX
Crystal Structure of bifunctional Kunitz type Trypsin /amylase inhibitor (AMTIN) from the tubers of Alocasia macrorrhiza
Summary for 5WVX
| Entry DOI | 10.2210/pdb5wvx/pdb |
| Related | 1AVA |
| Descriptor | Trypsin/chymotrypsin inhibitor, 2-acetamido-2-deoxy-beta-D-galactopyranose, CITRIC ACID (3 entities in total) |
| Functional Keywords | kunitz type trypsin inhibitor, alpha amylase inhibitor, hydrolase inhibitor |
| Biological source | Alocasia macrorrhizos (Giant taro) |
| Total number of polymer chains | 2 |
| Total formula weight | 40412.94 |
| Authors | Palayam, M.,Radhakrishnan, M.,Lakshminarayanan, K.,Balu, K.E.,Ganapathy, J.,Krishnasamy, G. (deposition date: 2016-12-29, release date: 2018-06-13, Last modification date: 2024-11-06) |
| Primary citation | Palayam, M.,Ganapathy, J.,Balu, K.E.,Pennathur, G.,Krishnasamy, G. Structural insights into a multifunctional inhibitor, 'AMTIN' from tubers of Alocasia macrorrhizos and its possible role in dengue protease (NS2B-NS3) inhibition. Int. J. Biol. Macromol., 113:681-691, 2018 Cited by PubMed Abstract: Protease inhibitors from plants play major role in defensive mechanism against various pathogenic organisms. AMTIN from the tubers of Alocasia macrorrhiza has been purified and characterized as multi-functional Kunitz type protease inhibitor. AMTIN is varied from other KTIs by having three different loops specific for binding to trypsin/amylase and subtilisin that are located approximately 30Ǻ away from one another as evidenced from crystallographic efforts. Biochemical studies on AMTIN reveal simultaneous binding of protease/amylase and have been cross validated using in-silico tools to model Amylase - AMTIN - Trypsin complex without any steric clashes. Apart from multi functionality, the remarkable structural and functional stability of AMTIN at high temperature, presence of many phosphorylation, myristoylation and glycosylation sites and molecular docking studies with dengue viral protease (NS2B-NS3) makes this protein interesting. Hence AMTIN can be considered as a template to design effective antivirals against dengue virus. PubMed: 29505868DOI: 10.1016/j.ijbiomac.2018.03.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.003 Å) |
Structure validation
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