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3a1h
From Proteopedia
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| - | [[Image:3a1h.png|left|200px]] | ||
| - | + | ==Crystal Structure Analysis of the Collagen-like Peptide, (PPG)4-OTG-(PPG)4== | |
| - | + | <StructureSection load='3a1h' size='340' side='right'caption='[[3a1h]], [[Resolution|resolution]] 1.08Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | or the | + | <table><tr><td colspan='2'>[[3a1h]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A1H FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></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=3a1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1h OCA], [https://pdbe.org/3a1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a1h RCSB], [https://www.ebi.ac.uk/pdbsum/3a1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a1h ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The single-crystal structures of three collagen-like host-guest peptides, (Pro-Pro-Gly)(4) -Hyp-Yaa-Gly-(Pro-Pro-Gly)(4) [Yaa = Thr, Val, Ser; Hyp = (4R)-4-hydroxyproline] were analyzed at atomic resolution. These peptides adopted a 7/2-helical structure similar to that of the (Pro-Pro-Gly)(9) peptide. The stability of these triple helices showed a similar tendency to that observed in Ac-(Gly-Hyp-Yaa)(10) -NH(2) (Yaa = Thr, Val, Ser) peptides. On the basis of their detailed structures, the differences in the triple-helical stabilities of the peptides containing a Hyp-Thr-Gly, Hyp-Val-Gly, or Hyp-Ser-Gly sequence were explained in terms of van der Waals interactions and dipole-dipole interaction between the Hyp residue in the X position and the Yaa residue in the Y position involved in the Hyp(X):Yaa(Y) stacking pair. This idea also explains the inability of Ac-(Gly-Hyp-alloThr)(10) -NH(2) and Ac-(Gly-Hyp-Ala)(10) -NH(2) peptides to form triple helices. In the Hyp(X):Thr(Y), Hyp(X):Val(Y), and Hyp(X):Ser(Y) stacking pairs, the proline ring of the Hyp residues adopts an up-puckering conformation, in agreement with the residual preference of Hyp, but in disagreement with the positional preference of X in the Gly-Xaa-Yaa sequence. (c) 2011 Wiley Periodicals, Inc. Biopolymers 95: 628-640, 2011. | ||
| - | + | Stabilization of triple-helical structures of collagen peptides containing a Hyp-Thr-Gly, Hyp-Val-Gly, or Hyp-Ser-Gly sequence.,Okuyama K, Miyama K, Morimoto T, Masakiyo K, Mizuno K, Bachinger HP Biopolymers. 2011 Sep;95(9):628-40. doi: 10.1002/bip.21625. Epub 2011 Mar, 25. PMID:21442606<ref>PMID:21442606</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3a1h" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
| - | + | [[Category: Bachinger HP]] | |
| - | + | [[Category: Miyama K]] | |
| - | == | + | [[Category: Mizuno K]] |
| - | < | + | [[Category: Okuyama K]] |
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Current revision
Crystal Structure Analysis of the Collagen-like Peptide, (PPG)4-OTG-(PPG)4
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