1EWS
THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1
Summary for 1EWS
| Entry DOI | 10.2210/pdb1ews/pdb |
| Descriptor | RK-1 DEFENSIN (1 entity in total) |
| Functional Keywords | alpha defensin, triple-stranded beta-sheet, antimicrobial protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 3712.39 |
| Authors | McManus, A.M.,Dawson, N.F.,Wade, J.D.,Craik, D.J. (deposition date: 2000-04-26, release date: 2001-05-02, Last modification date: 2024-11-20) |
| Primary citation | McManus, A.M.,Dawson, N.F.,Wade, J.D.,Carrington, L.E.,Winzor, D.J.,Craik, D.J. Three-dimensional structure of RK-1: a novel alpha-defensin peptide. Biochemistry, 39:15757-15764, 2000 Cited by PubMed Abstract: 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. PubMed: 11123900DOI: 10.1021/bi000457l PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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