1k6f
From Proteopedia
(New page: 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 11:30, 21 February 2008
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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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