1k6f: Difference between revisions

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[[~~Image~~:1k6f.~~png|left|200px~~]]

==Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3==

== 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>

== 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.

~~{{STRUCTURE_1k6f| PDB=1k6f | SCENE= }}~~

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>

~~===Crystal Structure~~ of the ~~Collagen Triple Helix Model [(Pro-Pro-Gly)10]3===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_11790836}}~~

~~==About this Structure==~~

~~[[1k6f]] is a 6 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=1K6F OCA].~~

==See Also==

*[[Collagen|Collagen]]

== References ==

==~~Reference~~==

<~~ref group="xtra">PMID:011790836<~~/~~ref~~><~~references group="xtra"~~/>

__TOC__

</StructureSection>

[[Category: Berisio, R.]]

[[Category: Mazzarella, L.]]

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@@ Line 1: / Line 1: @@
-[[Image:1k6f.png|left|200px]]
+==Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3==
+<StructureSection load='1k6f' size='340' side='right' caption='[[1k6f]], [[Resolution|resolution]] 1.30&Aring;' 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.
-{{STRUCTURE_1k6f|  PDB=1k6f  |  SCENE=  }}
+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>
-===Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11790836}}
-==About this Structure==
-[[1k6f]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6F OCA].
 ==See Also==
 *[[Collagen|Collagen]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011790836</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Berisio, R.]]
 [[Category: Mazzarella, L.]]