1tv0 | pdb_00001tv0

Solution structure of cryptdin-4, the most potent alpha-defensin from mouse Paneth cells

spinqualitylabelsall models 1tv0, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tv0 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: DEFCR4 (Mus musculus) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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