1ews
From Proteopedia
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| - | + | ==THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1== | |
| - | + | <StructureSection load='1ews' size='340' side='right' caption='[[1ews]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[1ews]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EWS FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1ews RCSB], [http://www.ebi.ac.uk/pdbsum/1ews PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:11123900</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Defensin|Defensin]] | *[[Defensin|Defensin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | [[Category: Craik, D J | + | [[Category: Craik, D J]] |
| - | [[Category: Dawson, N F | + | [[Category: Dawson, N F]] |
| - | [[Category: McManus, A M | + | [[Category: McManus, A M]] |
| - | [[Category: Wade, J D | + | [[Category: Wade, J D]] |
[[Category: Alpha defensin]] | [[Category: Alpha defensin]] | ||
[[Category: Antimicrobial protein]] | [[Category: Antimicrobial protein]] | ||
[[Category: Triple-stranded beta-sheet]] | [[Category: Triple-stranded beta-sheet]] | ||
Revision as of 13:47, 17 December 2014
THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1
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