1tv0
From Proteopedia
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Solution structure of cryptdin-4, the most potent alpha-defensin from mouse Paneth cells
Overview
Mammalian defensins are abundant antimicrobial peptides that contribute to, host defense. They are characterized by several conserved amino acids, including six invariant cysteine residues which form three intramolecular, disulfide bonds and stabilize the tertiary structure. Cryptdin-4 (Crp4), a, mouse alpha-defensin with potent in vitro bactericidal activity, has a, primary structure distinct from all known alpha-defensins in that its, polypeptide backbone uniquely lacks three residues between Cys(IV) and, Cys(V). NMR diffusion experiments showed that Crp4 is monomeric in, solution, and its three-dimensional solution structure, determined by, two-dimensional proton NMR, consists of a triple-stranded antiparallel, beta-sheet with the beta-strands joined to each other by a series of tight, turns and a beta-hairpin. However, the overall beta-sheet content in Crp4, is lower than that of other alpha-defensin structures, while the shape and, orientation of the Crp4 beta-hairpin also differ from those of other, alpha-defensin structures. These structural characteristics combined with, the high overall cationicity of Crp4 may contribute to its broad, bactericidal spectrum and membrane disruptive activity.
About this Structure
1TV0 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Solution structure of cryptdin-4, a mouse paneth cell alpha-defensin., Jing W, Hunter HN, Tanabe H, Ouellette AJ, Vogel HJ, Biochemistry. 2004 Dec 21;43(50):15759-66. PMID:15595831
Page seeded by OCA on Wed Nov 21 03:36:56 2007
