1cgd: Difference between revisions

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{{Seed}}
[[Image:1cgd.png|left|200px]]


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==HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE==
The line below this paragraph, containing "STRUCTURE_1cgd", creates the "Structure Box" on the page.
<StructureSection load='1cgd' size='340' side='right'caption='[[1cgd]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1cgd]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CGD FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr>
{{STRUCTURE_1cgd|  PDB=1cgd  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgd OCA], [https://pdbe.org/1cgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cgd RCSB], [https://www.ebi.ac.uk/pdbsum/1cgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cgd ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: The collagen triple helix is a unique protein motif defined by the supercoiling of three polypeptide chains in a polyproline II conformation. It is a major domain of all collagen proteins and is also reported to exist in proteins with host defense function and in several membrane proteins. The triple-helical domain has distinctive properties. Collagen requires a high proportion of the post-translationally modified imino acid 4-hydroxyproline and water to stabilize its conformation and assembly. The crystal structure of a collagen-like peptide determined to 1.85 Angstrum showed that these two features may be related. RESULTS: A detailed analysis of the hydration structure of the collagen-like peptide is presented. The water molecules around the carbonyl and hydroxyprolyl groups show distinctive geometries. There are repetitive patterns of water bridges that link oxygen atoms within a single peptide chain, between different chains and between different triple helices. Overall, the water molecules are organized in a semi-clathrate-like structure that surrounds and interconnects triple helices in the crystal lattice. Hydroxyprolyl groups play a crucial role in the assembly. CONCLUSIONS: The roles of hydroxyproline and hydration are strongly interrelated in the structure of the collagen triple helix. The specific, repetitive water bridges observed in this structure buttress the triple-helical conformation. The extensively ordered hydration structure offers a good model for the interpretation of the experimental results on collagen stability and assembly.


===HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE===
Hydration structure of a collagen peptide.,Bella J, Brodsky B, Berman HM Structure. 1995 Sep 15;3(9):893-906. PMID:8535783<ref>PMID:8535783</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_8535783}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1cgd" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 8535783 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_8535783}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGD OCA].
[[Category: Bella J]]
 
[[Category: Berman HM]]
==Reference==
[[Category: Brodsky B]]
Hydration structure of a collagen peptide., Bella J, Brodsky B, Berman HM, Structure. 1995 Sep 15;3(9):893-906. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535783 8535783]
[[Category: Bella, J.]]
[[Category: Berman, H M.]]
[[Category: Brodsky, B.]]
[[Category: Collagen]]
[[Category: Collagen hydration]]
[[Category: Connective tissue]]
[[Category: Extracellular matrix]]
[[Category: Hydroxyproline]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:42:46 2008''

Latest revision as of 11:22, 2 August 2023

HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE

1cgd, resolution 1.85Å

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