1cgd
From Proteopedia
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| - | [[Image:1cgd.gif|left|200px]] | + | [[Image:1cgd.gif|left|200px]] |
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| - | '''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE''' | + | {{Structure |
| + | |PDB= 1cgd |SIZE=350|CAPTION= <scene name='initialview01'>1cgd</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CGD is a [ | + | 1CGD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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:// | + | 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: Protein complex]] | ||
[[Category: Bella, J.]] | [[Category: Bella, J.]] | ||
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[[Category: hydroxyproline]] | [[Category: hydroxyproline]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:04 2008'' |
Revision as of 08:24, 20 March 2008
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| , resolution 1.85Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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 Thu Mar 20 10:24:04 2008
