1cgd
From Proteopedia
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[[Image:1cgd.gif|left|200px]] | [[Image:1cgd.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1cgd| PDB=1cgd | SCENE= }} | |
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'''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE''' | '''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGD OCA]. | |
==Reference== | ==Reference== | ||
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] | 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: Protein complex]] | ||
[[Category: Bella, J.]] | [[Category: Bella, J.]] | ||
[[Category: Berman, H M.]] | [[Category: Berman, H M.]] | ||
[[Category: Brodsky, B.]] | [[Category: Brodsky, B.]] | ||
| - | [[Category: | + | [[Category: Collagen]] |
| - | [[Category: | + | [[Category: Collagen hydration]] |
| - | [[Category: | + | [[Category: Connective tissue]] |
| - | [[Category: | + | [[Category: Extracellular matrix]] |
| - | [[Category: | + | [[Category: Hydroxyproline]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:42:28 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:42, 2 May 2008
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
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 Page seeded by OCA on Fri May 2 12:42:28 2008
