1cvo
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvo OCA], [http://www.ebi.ac.uk/pdbsum/1cvo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cvo RCSB]</span> | ||
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[[Category: cytotoxin]] | [[Category: cytotoxin]] | ||
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Revision as of 16:29, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA
Overview
Cardiotoxins are small proteins that are found in the venoms of snakes from the Elapidae family. These toxins are known to bind to and disrupt the organization, integrity, and function of the cell membrane. Most of the well-studied cardiotoxins cause depolarization of membrane potentials and/or lysis of red cells. In contrast, CTX V from Naja naja atra displays poor hemolytic activity but is proficient at inducing aggregation and fusion of sphingomyelin vesicles [Chien et al. (1991) J. Biol. Chem. 266, 3252-3259]. To determine whether the unique activity of this CTX is attributable to its tertiary structure, the solution structure of CTX V was determined by NMR methods. On the basis of these studies, this cardiotoxin has the same general topology as other members of the family, and thus its unusual properties do not arise from any gross structural differences that are detectable by solution NMR methods. Molecular dynamics calculations indicate that residues 36-50 show concerted fluctuations. On the basis of sequence similarity, we postulate that residues 30-34 are important in determining the specificity of cardiotoxins for fusion versus lysis of vesicles.
About this Structure
1CVO is a Single protein structure of sequence from Naja atra. Full crystallographic information is available from OCA.
Reference
Solution structure of cardiotoxin V from Naja naja atra., Singhal AK, Chien KY, Wu WG, Rule GS, Biochemistry. 1993 Aug 10;32(31):8036-44. PMID:8347605
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