1imt
From Proteopedia
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| - | [[Image:1imt.gif|left|200px]] | + | [[Image:1imt.gif|left|200px]] |
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| - | '''MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1imt |SIZE=350|CAPTION= <scene name='initialview01'>1imt</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IMT is a [ | + | 1IMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMT OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9761684 9761684] |
[[Category: Dendroaspis polylepis polylepis]] | [[Category: Dendroaspis polylepis polylepis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Schweitz, H.]] | [[Category: Schweitz, H.]] | ||
[[Category: contract guinea pig ileum]] | [[Category: contract guinea pig ileum]] | ||
| - | [[Category: resistance to | + | [[Category: resistance to endoprotease]] |
[[Category: structural homologue of colipase]] | [[Category: structural homologue of colipase]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:23 2008'' |
Revision as of 09:52, 20 March 2008
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MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES
Overview
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.
About this Structure
1IMT is a Single protein structure of sequence from Dendroaspis polylepis polylepis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:52:23 2008
