1ews
From Proteopedia
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| - | [[Image:1ews.gif|left|200px]] | + | [[Image:1ews.gif|left|200px]] |
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| - | '''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1''' | + | {{Structure |
| + | |PDB= 1ews |SIZE=350|CAPTION= <scene name='initialview01'>1ews</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EWS is a [ | + | 1EWS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11123900 11123900] |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: triple-stranded beta-sheet]] | [[Category: triple-stranded beta-sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:17 2008'' |
Revision as of 09:01, 20 March 2008
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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
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