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


{{Structure
==THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1==
|PDB= 1ews |SIZE=350|CAPTION= <scene name='initialview01'>1ews</scene>
<StructureSection load='1ews' size='340' side='right'caption='[[1ews]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1ews]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1EWS FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ews FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ews OCA], [https://pdbe.org/1ews PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ews RCSB], [https://www.ebi.ac.uk/pdbsum/1ews PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ews ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/RK1_RABIT RK1_RABIT] Has antimicrobial activity against E.coli and activates ion channel activity.
<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.


'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ews" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Defensin 3D structures|Defensin 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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: Craik DJ]]
[[Category: Craik, D J.]]
[[Category: Dawson NF]]
[[Category: Dawson, N F.]]
[[Category: McManus AM]]
[[Category: McManus, A M.]]
[[Category: Wade JD]]
[[Category: Wade, J D.]]
[[Category: alpha defensin]]
[[Category: triple-stranded beta-sheet]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:17 2008''
Retrieved from "https://proteopedia.org/1ews"