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2atg
From Proteopedia
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| - | [[ | + | ==NMR structure of Retrocyclin-2 in SDS== |
| + | <StructureSection load='2atg' size='340' side='right' caption='[[2atg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2atg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ATG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ATG FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2atg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2atg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2atg RCSB], [http://www.ebi.ac.uk/pdbsum/2atg PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Retrocyclins are circular mini-defensins with significant potential as agents against human immunodeficiency virus, influenza A, and herpes simplex virus. Retrocyclins bind carbohydrate-containing surface molecules such as gp120 and CD4 with high affinity (Kd, 10-100 nM), promoting their localization on cell membranes. The structural features important for activity have yet to be fully elucidated, but here, we have determined the first three-dimensional structure of a retrocyclin, namely, one of the most potent forms, retrocyclin-2. In the presence of SDS micelles, a well-defined beta-hairpin braced by three disulfide bonds that defines the cystine ladder motif is present. By contrast, a well-defined structure could not be determined in aqueous solution, suggesting that the presence of SDS micelles stabilizes the extended conformation of retrocyclin-2. Translational diffusion measurements indicate that retrocyclin-2 interacts with the SDS micelles, and such a membrane-like interaction may be an important feature in the mechanism of action of these antimicrobial peptides. Analytical ultracentrifugation and the NMR data indicated that retrocyclin-2 self-associates to form a trimer in a concentration-dependent manner. The ability to self-associate may contribute to the high-affinity binding of retrocyclins for glycoproteins by increasing the valency and enhancing the ability of retrocyclins to cross-link cell surface glycoproteins. | ||
| - | + | Retrocyclin-2: structural analysis of a potent anti-HIV theta-defensin.,Daly NL, Chen YK, Rosengren KJ, Marx UC, Phillips ML, Waring AJ, Wang W, Lehrer RI, Craik DJ Biochemistry. 2007 Sep 4;46(35):9920-8. Epub 2007 Aug 8. PMID:17685559<ref>PMID:17685559</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Chen, Y K.]] | [[Category: Chen, Y K.]] | ||
[[Category: Craik, D J.]] | [[Category: Craik, D J.]] | ||
Revision as of 06:53, 9 June 2014
NMR structure of Retrocyclin-2 in SDS
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