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| | <StructureSection load='5wvx' size='340' side='right'caption='[[5wvx]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='5wvx' size='340' side='right'caption='[[5wvx]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wvx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Alocasia_macrorrhizos Alocasia macrorrhizos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WVX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WVX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wvx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alocasia_macrorrhizos Alocasia macrorrhizos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WVX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.003Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ava|1ava]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wvx OCA], [http://pdbe.org/5wvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wvx RCSB], [http://www.ebi.ac.uk/pdbsum/5wvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wvx ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5wvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wvx OCA], [https://pdbe.org/5wvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wvx RCSB], [https://www.ebi.ac.uk/pdbsum/5wvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wvx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ITC_ALOMA ITC_ALOMA]] Inhibits trypsin and alpha-chymotrypsin. | + | [https://www.uniprot.org/uniprot/ITC_ALOMA ITC_ALOMA] Inhibits trypsin and alpha-chymotrypsin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Alocasia macrorrhizos]] | | [[Category: Alocasia macrorrhizos]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Balu, K E]] | + | [[Category: Balu KE]] |
| - | [[Category: Ganapathy, J]] | + | [[Category: Ganapathy J]] |
| - | [[Category: Krishnasamy, G]] | + | [[Category: Krishnasamy G]] |
| - | [[Category: Lakshminarayanan, K]] | + | [[Category: Lakshminarayanan K]] |
| - | [[Category: Palayam, M]] | + | [[Category: Palayam M]] |
| - | [[Category: Radhakrishnan, M]] | + | [[Category: Radhakrishnan M]] |
| - | [[Category: Alpha amylase inhibitor]]
| + | |
| - | [[Category: Hydrolase inhibitor]]
| + | |
| - | [[Category: Kunitz type trypsin inhibitor]]
| + | |
| Structural highlights
Function
ITC_ALOMA Inhibits trypsin and alpha-chymotrypsin.
Publication Abstract from PubMed
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 30A 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.
Structural insights into a multifunctional inhibitor, 'AMTIN' from tubers of Alocasia macrorrhizos and its possible role in dengue protease (NS2B-NS3) inhibition.,Palayam M, Ganapathy J, Balu KE, Pennathur G, Krishnasamy G Int J Biol Macromol. 2018 Jul 1;113:681-691. doi: 10.1016/j.ijbiomac.2018.03.010., Epub 2018 Mar 2. PMID:29505868[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Palayam M, Ganapathy J, Balu KE, 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. 2018 Jul 1;113:681-691. doi: 10.1016/j.ijbiomac.2018.03.010., Epub 2018 Mar 2. PMID:29505868 doi:http://dx.doi.org/10.1016/j.ijbiomac.2018.03.010
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