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| - | [[Image:1ews.gif|left|200px]] | |
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| - | {{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®/PubMed®, 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''
| + | |
| Structural highlights
Function
RK1_RABIT Has antimicrobial activity against E.coli and activates ion channel activity.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McManus AM, Dawson NF, Wade JD, Carrington LE, Winzor DJ, Craik DJ. Three-dimensional structure of RK-1: a novel alpha-defensin peptide. Biochemistry. 2000 Dec 26;39(51):15757-64. PMID:11123900
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