1cgd: Difference between revisions
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=" | [[Image:1cgd.gif|left|200px]]<br /><applet load="1cgd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1cgd, resolution 1.85Å" /> | caption="1cgd, resolution 1.85Å" /> | ||
'''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE'''<br /> | '''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: The collagen triple helix is a unique protein motif defined by | 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== | ==About this Structure== | ||
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:// | 1CGD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bella, J.]] | [[Category: Bella, J.]] | ||
[[Category: Berman, H | [[Category: Berman, H M.]] | ||
[[Category: Brodsky, B.]] | [[Category: Brodsky, B.]] | ||
[[Category: ACY]] | [[Category: ACY]] | ||
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[[Category: hydroxyproline]] | [[Category: hydroxyproline]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:48 2008'' | ||
Revision as of 10:05, 21 February 2008
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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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