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[[Image:1ews.gif|left|200px]]
[[Image:1ews.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ews FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ews OCA], [http://www.ebi.ac.uk/pdbsum/1ews PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ews RCSB]</span>
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'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1'''
'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1'''
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[[Category: McManus, A M.]]
[[Category: McManus, A M.]]
[[Category: Wade, J D.]]
[[Category: Wade, J D.]]
[[Category: alpha defensin]]
[[Category: Alpha defensin]]
[[Category: triple-stranded beta-sheet]]
[[Category: Triple-stranded beta-sheet]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:36:35 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:11:08 2008''

Revision as of 12:36, 2 May 2008

File:1ews.gif

Template:STRUCTURE 1ews

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 Fri May 2 15:36:35 2008

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