3b0s: Difference between revisions
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[[ | ==Crystal Structure of (Gly-Pro-Hyp)9== | ||
<StructureSection load='3b0s' size='340' side='right' caption='[[3b0s]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3b0s]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B0S FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v7h|1v7h]], [[1v4f|1v4f]], [[3ah9|3ah9]]</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=3b0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b0s RCSB], [http://www.ebi.ac.uk/pdbsum/3b0s PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Collagens have long been believed to adopt a triple-stranded molecular structure with a 10/3 symmetry (ten triplet units in three turns) and an axial repeat of 29 A. This belief even persisted after an alternative structure with a 7/2 symmetry (seven triplet units in two turns) with an axial repeat of 20 A had been proposed. The uncertainty regarding the helical symmetry of collagens is attributed to inadequate X-ray fiber diffraction data. Therefore, for better understanding of the collagen helix, single-crystal analyses of peptides with simplified characteristic amino acid sequences and similar compositions to collagens have long been awaited. Here we report the crystal structure of (Gly-Pro-Hyp)(9) peptide at a resolution of 1.45 A. The repeating unit of this peptide, Gly-Pro-Hyp, is the most typical sequence present in collagens, and it has been used as a basic repeating unit in fiber diffraction analyses of collagen. The (Gly-Pro-Hyp)(9) peptide adopts a triple-stranded structure with an average helical symmetry close to the ideal 7/2 helical model for collagen. This observation strongly suggests that the average molecular structure of collagen is not the accepted Rich and Crick 10/3 helical model but is a 7/2 helical conformation. (c) 2012 Wiley Periodicals, Inc. Biopolymers 97: 607-616, 2012. | |||
Crystal structure of (Gly-Pro-Hyp)(9) : Implications for the collagen molecular model.,Okuyama K, Miyama K, Mizuno K, Bachinger HP Biopolymers. 2012 Aug;97(8):607-16. doi: 10.1002/bip.22048. PMID:22605552<ref>PMID:22605552</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
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[[Category: Bachinger, H P.]] | [[Category: Bachinger, H P.]] | ||
[[Category: Miyama, K.]] | [[Category: Miyama, K.]] | ||
Revision as of 11:06, 14 May 2014
Crystal Structure of (Gly-Pro-Hyp)9
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