1k6f: Difference between revisions

Revision as of 09:51, 2 July 2008

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File:1k6f.png

Template:STRUCTURE 1k6f

Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3

Template:ABSTRACT PUBMED 11790836

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)., Berisio R, Vitagliano L, Mazzarella L, Zagari A, Protein Sci. 2002 Feb;11(2):262-70. PMID:11790836

Page seeded by OCA on Wed Jul 2 09:51:15 2008

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OCA

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-'''Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3'''
+===Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3===
-==Overview==
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-The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)(10)](3) is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 A, using synchrotron radiation. The final model, which was refined to an R(factor) of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)(10)](3) packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.
+The line below this paragraph, {{ABSTRACT_PUBMED_11790836}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Puckering]]
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