1k6f: Difference between revisions

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[[Image:1k6f.jpg|left|200px]]<br /><applet load="1k6f" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1k6f.jpg|left|200px]]<br /><applet load="1k6f" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1k6f, resolution 1.3Å" />

'''Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1K6F OCA].

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==

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[[Category: triple helix]]

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@@ Line 1: / Line 1: @@
-[[Image:1k6f.jpg|left|200px]]<br /><applet load="1k6f" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k6f.jpg|left|200px]]<br /><applet load="1k6f" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k6f, resolution 1.3&Aring;" />
 '''Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3'''<br />
 ==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.
+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==
-K6F 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K6F OCA].
+K6F 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==
@@ Line 21: / Line 21: @@
 [[Category: triple helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:49:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:37 2008''