1k6f
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<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.ebi.ac.uk/pdbsum/1k6f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k6f RCSB]</span> | ||
}} | }} | ||
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[[Category: collagen stability]] | [[Category: collagen stability]] | ||
[[Category: puckering]] | [[Category: puckering]] | ||
- | [[Category: triple helix]] | + | [[Category: triple helix,]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:03 2008'' |
Revision as of 18:44, 30 March 2008
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, resolution 1.3Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3
Overview
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.
About this Structure
1K6F is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
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