1k6f: Difference between revisions
New page: left|200px<br /><applet load="1k6f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k6f, resolution 1.3Å" /> '''Crystal Structure of ... |
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[[Image:1k6f.jpg|left|200px]]<br /><applet load="1k6f" size=" | [[Image:1k6f.jpg|left|200px]]<br /><applet load="1k6f" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1k6f, resolution 1.3Å" /> | caption="1k6f, resolution 1.3Å" /> | ||
'''Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3'''<br /> | '''Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3'''<br /> | ||
==Overview== | ==Overview== | ||
The first report of the full-length structure of the collagen-like | 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== | ==About this Structure== | ||
1K6F is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1K6F is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6F OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: triple helix]] | [[Category: triple helix]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:37 2008'' | ||
Revision as of 14:30, 21 February 2008
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Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3
OverviewOverview
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 StructureAbout this Structure
1K6F is a Protein complex structure of sequences from [1]. 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
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