1k6f
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | [[ | + | ==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 09:16, 28 September 2014
Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3
|