1CVO

THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA

Summary for 1CVO

• Entry DOI: 10.2210/pdb1cvo/pdb
• Descriptor: CARDIOTOXIN V (1 entity in total)
• Functional Keywords: cytotoxin
• Biological source: Naja atra (Chinese cobra)
• Cellular location: Secreted : P62375
• Total number of polymer chains: 1
• Total formula weight: 7027.46

Authors

Singhal, A.K.,Chien, K.-Y.,Wu, W.-G.,Rule, G.S. (deposition date: 1993-04-28, release date: 1994-01-31, Last modification date: 2017-11-29)

Primary citation

Singhal, A.K.,Chien, K.Y.,Wu, W.G.,Rule, G.S.
Solution structure of cardiotoxin V from Naja naja atra.
Biochemistry, 32:8036-8044, 1993

PubMed Abstract: 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.

PubMed: 8347605
DOI: 10.1021/bi00082a026

Experimental method

SOLUTION NMR