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3abn
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of (Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 at 1.02 A== | |
| - | === | + | <StructureSection load='3abn' size='340' side='right' caption='[[3abn]], [[Resolution|resolution]] 1.02Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3abn]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ABN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ABN FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a08|3a08]], [[3a19|3a19]], [[3a0m|3a0m]], [[2drx|2drx]], [[2drt|2drt]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3abn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3abn RCSB], [http://www.ebi.ac.uk/pdbsum/3abn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The single-crystal structure of the collagen-like peptide (Pro-Pro-Gly)4 -Hyp-Asp-Gly-(Pro-Pro-Gly)4 , was analyzed at 1.02 A resolution. The overall average helical twist (theta = 49.6 degrees ) suggests that this peptide adopts a 7/2 triple-helical structure and that its conformation is very similar to that of (Gly-Pro-Hyp)9 , which has the typical repeating sequence in collagen. High-resolution studies on other collagen-like peptides have shown that imino acid-rich sequences preferentially adopt a 7/2 triple-helical structure (theta = 51.4 degrees ), whereas imino acid-lean sequences adopt relaxed conformations (theta < 51.4 degrees ). The guest Gly-Hyp-Asp sequence in the present peptide, however, has a large helical twist (theta = 61.1 degrees ), whereas that of the host Pro-Pro-Gly sequence is small (theta = 46.7 degrees ), indicating that the relationship between the helical conformation and the amino acid sequence of such peptides is complex. In the present structure, a strong intermolecular hydrogen bond between two Asp residues on the A and B strands might induce the large helical twist of the guest sequence; this is compensated by a reduced helical twist in the host, so that an overall 7/2-helical symmetry is maintained. The Asp residue in the C strand might interact electrostatically with the N-terminus of an adjacent molecule, causing axial displacement, reminiscent of the D-staggered structure in fibrous collagens. (c) 2013 Wiley Periodicals, Inc. Biopolymers 99: 436-447, 2013. | ||
| - | + | Crystal structure of the collagen model peptide (Pro-Pro-Gly)4 -Hyp-Asp-Gly-(Pro-Pro-Gly)4 at 1.0 A resolution.,Okuyama K, Kawaguchi T, Shimura M, Noguchi K, Mizuno K, Bachinger HP Biopolymers. 2013 Jul;99(7):436-47. doi: 10.1002/bip.22198. PMID:23616212<ref>PMID:23616212</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Bachinger, H P | + | == References == |
| - | [[Category: Kawaguchi, T | + | <references/> |
| - | [[Category: Mizuno, K | + | __TOC__ |
| - | [[Category: Noguchi, K | + | </StructureSection> |
| - | [[Category: Okuyama, K | + | [[Category: Bachinger, H P]] |
| - | [[Category: Shimura, M | + | [[Category: Kawaguchi, T]] |
| + | [[Category: Mizuno, K]] | ||
| + | [[Category: Noguchi, K]] | ||
| + | [[Category: Okuyama, K]] | ||
| + | [[Category: Shimura, M]] | ||
[[Category: Collagen-helix]] | [[Category: Collagen-helix]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
Revision as of 17:49, 21 December 2014
Crystal structure of (Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 at 1.02 A
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