3abn

</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"><div style='overflow: auto; max-height: 3em;'>[[3a08|3a08]], [[3a19|3a19]], [[3a0m|3a0m]], [[2drx|2drx]], [[2drt|2drt]]</div></td></tr>

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== 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 &lt; 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3abn" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bachinger, H P]]

[[Category: Kawaguchi, T]]

[[Category: Mizuno, K]]

[[Category: Noguchi, K]]

[[Category: Okuyama, K]]

[[Category: Shimura, M]]

[[Category: Structural protein]]