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2cuo

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{{Seed}}
 
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[[Image:2cuo.png|left|200px]]
 
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==Collagen model peptide (PRO-PRO-GLY)9==
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The line below this paragraph, containing "STRUCTURE_2cuo", creates the "Structure Box" on the page.
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<StructureSection load='2cuo' size='340' side='right'caption='[[2cuo]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_2cuo| PDB=2cuo | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q80BK4_SHV2 Q80BK4_SHV2]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Collagen model peptide (PRO-PRO-GLY)9===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2cuo" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16091587}}, adds the Publication Abstract to the page
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*[[Collagen 3D structures|Collagen 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16091587 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16091587}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CUO OCA].
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[[Category: Saimiriine gammaherpesvirus 2]]
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[[Category: Hongo C]]
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==Reference==
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[[Category: Nishino N]]
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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]
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[[Category: Noguchi K]]
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[[Category: Hongo, C.]]
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[[Category: Okuyama K]]
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[[Category: Nishino, N.]]
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[[Category: Tanaka Y]]
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[[Category: Noguchi, K.]]
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[[Category: Okuyama, K.]]
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[[Category: Tanaka, Y.]]
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[[Category: Collagen model peptide]]
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[[Category: Puckering]]
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[[Category: Triple-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:05:15 2008''
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Current revision

Collagen model peptide (PRO-PRO-GLY)9

PDB ID 2cuo

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