1imt
From Proteopedia
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| - | [[Image:1imt.gif|left|200px]] | ||
| - | + | ==MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES== | |
| - | + | <StructureSection load='1imt' size='340' side='right'caption='[[1imt]]' scene=''> | |
| - | | | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1imt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IMT FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 39 models</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=1imt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1imt OCA], [https://pdbe.org/1imt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1imt RCSB], [https://www.ebi.ac.uk/pdbsum/1imt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1imt ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/MIT1_DENPO MIT1_DENPO] Potently contracts gastrointestinal (GI) smooth muscle. The receptor for this toxin is present both in the CNS and in the smooth muscle and may be a potassium channel.<ref>PMID:10567694</ref> | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | == | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/1imt_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1imt ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The solution structure of mamba intestinal toxin 1 (MIT1), isolated from Dendroaspis polylepis polylepis venom, has been determined. This molecule is a cysteine-rich polypeptide exhibiting no recognised family membership. Resistance to MIT1 to classical specific endoproteases produced contradictory NMR and biochemical information concerning disulphide-bridge topology. We have used distance restraints allowing ambiguous partners between S atoms in combination with NMR-derived structural information, to correctly determine the disulphide-bridge topology. The resultant solution structure of MIT1, determined to a resolution of 0.5 A, reveals an unexpectedly similar global fold with respect to colipase, a protein involved in fatty acid digestion. Colipase exhibits an analogous resistance to endoprotease activity, indicating for the first time the possible topological origins of this biochemical property. The biochemical and structural homology permitted us to propose a mechanically related digestive function for MIT1 and provides novel information concerning snake venom protein evolution. | The solution structure of mamba intestinal toxin 1 (MIT1), isolated from Dendroaspis polylepis polylepis venom, has been determined. This molecule is a cysteine-rich polypeptide exhibiting no recognised family membership. Resistance to MIT1 to classical specific endoproteases produced contradictory NMR and biochemical information concerning disulphide-bridge topology. We have used distance restraints allowing ambiguous partners between S atoms in combination with NMR-derived structural information, to correctly determine the disulphide-bridge topology. The resultant solution structure of MIT1, determined to a resolution of 0.5 A, reveals an unexpectedly similar global fold with respect to colipase, a protein involved in fatty acid digestion. Colipase exhibits an analogous resistance to endoprotease activity, indicating for the first time the possible topological origins of this biochemical property. The biochemical and structural homology permitted us to propose a mechanically related digestive function for MIT1 and provides novel information concerning snake venom protein evolution. | ||
| - | + | A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis.,Boisbouvier J, Albrand JP, Blackledge M, Jaquinod M, Schweitz H, Lazdunski M, Marion D J Mol Biol. 1998;283(1):205-19. PMID:9761684<ref>PMID:9761684</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1imt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Dendroaspis polylepis polylepis]] | [[Category: Dendroaspis polylepis polylepis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Albrand | + | [[Category: Albrand J-P]] |
| - | [[Category: Blackledge | + | [[Category: Blackledge M]] |
| - | [[Category: Boisbouvier | + | [[Category: Boisbouvier J]] |
| - | [[Category: Jaquinod | + | [[Category: Jaquinod M]] |
| - | [[Category: Lazdunski | + | [[Category: Lazdunski M]] |
| - | [[Category: Marion | + | [[Category: Marion D]] |
| - | [[Category: Schweitz | + | [[Category: Schweitz H]] |
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Current revision
MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES
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