1cgd
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(New page: 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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Revision as of 23:22, 24 November 2007
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HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE
Overview
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
1CGD is a Protein complex structure of sequences from [1] with ACY as ligand. Full crystallographic information is available from OCA.
Reference
Hydration structure of a collagen peptide., Bella J, Brodsky B, Berman HM, Structure. 1995 Sep 15;3(9):893-906. PMID:8535783
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