1ews
From Proteopedia
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THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1
Overview
NMR spectroscopy and simulated annealing calculations have been used to, determine the three-dimensional structure of RK-1, an antimicrobial, peptide from rabbit kidney recently discovered from homology screening, based on the distinctive physicochemical properties of the, corticostatins/defensins. RK-1 consists of 32 residues, including six, cysteines arranged into three disulfide bonds. It exhibits antimicrobial, activity against Escherichia coli and activates Ca(2+) channels in vitro., Through its physicochemical similarity, identical cysteine spacing, and, linkage to the corticostatins/defensins, it was presumed to be a member of, this family. However, RK-1 lacks both a large number of arginines in the, primary sequence and a high overall positive charge, which are, characteristic of this family of peptides. The three-dimensional solution, structure, determined by NMR, consists of a triple-stranded antiparallel, beta-sheet and a series of turns and is similar to the known structures of, other alpha-defensins. This has enabled the definitive classification of, RK-1 as a member of this family of antimicrobial peptides. Ultracentrifuge, measurements confirmed that like rabbit neutrophil defensins, RK-1 is, monomeric in solution, in contrast to human neutrophil defensins, which, are dimeric.
About this Structure
1EWS is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of RK-1: a novel alpha-defensin peptide., McManus AM, Dawson NF, Wade JD, Carrington LE, Winzor DJ, Craik DJ, Biochemistry. 2000 Dec 26;39(51):15757-64. PMID:11123900
Page seeded by OCA on Tue Nov 20 14:23:00 2007
