1imt
From Proteopedia
| |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 21:21:52 2008
