3a0m: Difference between revisions
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==Structure of (PPG)4-OVG-(PPG)4, monoclinic, twinned crystal== | |||
<StructureSection load='3a0m' size='340' side='right'caption='[[3a0m]], [[Resolution|resolution]] 1.02Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3a0m]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A0M 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]] 1.02Å</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=3a0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0m OCA], [https://pdbe.org/3a0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a0m RCSB], [https://www.ebi.ac.uk/pdbsum/3a0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a0m 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 3a0m" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Bachinger HP]] | |||
[[Category: Mizuno K]] | |||
[[Category: Morimoto T]] | |||
[[Category: Okuyama K]] | |||
Latest revision as of 14:06, 1 November 2023
Structure of (PPG)4-OVG-(PPG)4, monoclinic, twinned crystal
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