View source for 2atg


==NMR structure of Retrocyclin-2 in SDS==
<StructureSection load='2atg' size='340' side='right'caption='[[2atg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2atg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2ATG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2atg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2atg OCA], [https://pdbe.org/2atg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2atg RCSB], [https://www.ebi.ac.uk/pdbsum/2atg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2atg ProSAT]</span></td></tr>
</table>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen YK]]
[[Category: Craik DJ]]
[[Category: Daly NL]]
[[Category: Lehrer RI]]
[[Category: Marx UC]]
[[Category: Phillips ML]]
[[Category: Rosengren KJ]]
[[Category: Wang W]]
[[Category: Waring AJ]]