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New page: left|200px<br /><applet load="1cgd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cgd, resolution 1.85Å" /> '''HYDRATION STRUCTURE ...
 
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[[Image:1cgd.gif|left|200px]]<br /><applet load="1cgd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cgd, resolution 1.85&Aring;" />
'''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE'''<br />


==Overview==
==HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE==
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.
<StructureSection load='1cgd' size='340' side='right'caption='[[1cgd]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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.


==About this Structure==
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>
1CGD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CGD OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Hydration structure of a collagen peptide., Bella J, Brodsky B, Berman HM, Structure. 1995 Sep 15;3(9):893-906. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8535783 8535783]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1cgd" style="background-color:#fffaf0;"></div>
[[Category: Bella, J.]]
== References ==
[[Category: Berman, H.M.]]
<references/>
[[Category: Brodsky, B.]]
__TOC__
[[Category: ACY]]
</StructureSection>
[[Category: collagen]]
[[Category: Large Structures]]
[[Category: collagen hydration]]
[[Category: Bella J]]
[[Category: connective tissue]]
[[Category: Berman HM]]
[[Category: extracellular matrix]]
[[Category: Brodsky B]]
[[Category: hydroxyproline]]
 
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