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[[ | ==Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3== | ||
<StructureSection load='1k6f' size='340' side='right' caption='[[1k6f]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1k6f]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K6F 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=1k6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k6f RCSB], [http://www.ebi.ac.uk/pdbsum/1k6f PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:11790836</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Collagen|Collagen]] | *[[Collagen|Collagen]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Berisio, R.]] | [[Category: Berisio, R.]] | ||
[[Category: Mazzarella, L.]] | [[Category: Mazzarella, L.]] | ||
Revision as of 12:16, 28 September 2014
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
Structural highlights
Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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