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[[Image:2cuo.gif|left|200px]]
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{{STRUCTURE_2cuo|  PDB=2cuo  |  SCENE=  }}
'''Collagen model peptide (PRO-PRO-GLY)9'''


==Collagen model peptide (PRO-PRO-GLY)9==
<StructureSection load='2cuo' size='340' side='right'caption='[[2cuo]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cuo]] 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=2CUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CUO 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]] 1.33&#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=2cuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cuo OCA], [https://pdbe.org/2cuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cuo RCSB], [https://www.ebi.ac.uk/pdbsum/2cuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cuo 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 crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix.


==Overview==
Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3.,Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N J Biochem. 2005 Aug;138(2):135-44. PMID:16091587<ref>PMID:16091587</ref>
The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CUO OCA].
</div>
<div class="pdbe-citations 2cuo" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem. 2005 Aug;138(2):135-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16091587 16091587]
*[[Collagen 3D structures|Collagen 3D structures]]
[[Category: Hongo, C.]]
== References ==
[[Category: Nishino, N.]]
<references/>
[[Category: Noguchi, K.]]
__TOC__
[[Category: Okuyama, K.]]
</StructureSection>
[[Category: Tanaka, Y.]]
[[Category: Large Structures]]
[[Category: Collagen model peptide]]
[[Category: Saimiriine gammaherpesvirus 2]]
[[Category: Puckering]]
[[Category: Hongo C]]
[[Category: Triple-helix]]
[[Category: Nishino N]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 23:06:40 2008''
[[Category: Noguchi K]]
[[Category: Okuyama K]]
[[Category: Tanaka Y]]
Retrieved from "https://proteopedia.org/2cuo"