1k6f: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[1k6f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saimiriine_gammaherpesvirus_2 Saimiriine gammaherpesvirus 2]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1K6F FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6f OCA], [https://pdbe.org/1k6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k6f RCSB], [https://www.ebi.ac.uk/pdbsum/1k6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k6f ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6f OCA], [https://pdbe.org/1k6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k6f RCSB], [https://www.ebi.ac.uk/pdbsum/1k6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k6f ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/Q80BK4_SHV2 Q80BK4_SHV2]
-<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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1k6f" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Collagen 3D structures|Collagen 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>