1kfp
From Proteopedia
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Solution structure of the antimicrobial 18-residue gomesin
Overview
Gomesin is the first peptide isolated from spider exhibiting antimicrobial, activities. This highly cationic peptide is composed of 18 amino-acid, residues including four cysteines forming two disulfide linkages. The, solution structure of gomesin has been determined using proton, two-dimensional NMR (2D-NMR) and restrained molecular dynamics, calculations. The global fold of gomesin consists in a well-resolved, two-stranded antiparallel betasheet connected by a noncanonical betaturn., A comparison between the structures of gomesin and protegrin-1 from, porcine and androctonin from scorpion outlines several common features in, the distribution of hydrophobic and hydrophilic residues. The N- and, C-termini, the betaturn and one face of the betasheet are hydrophilic, but, the hydrophobicity of the other face depends on the peptide. The, similarities suggest that the molecules interact with membranes in an, analogous manner. The importance of the intramolecular disulfide bridges, in the biological activity of gomesin is being investigated.
About this Structure
1KFP is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider., Mandard N, Bulet P, Caille A, Daffre S, Vovelle F, Eur J Biochem. 2002 Feb;269(4):1190-8. PMID:11856345
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