1vdf
From Proteopedia
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[[Category: oligomeric matrix protein]] | [[Category: oligomeric matrix protein]] | ||
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Revision as of 14:13, 30 October 2007
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ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN
Overview
Oligomerization by the formation of alpha-helical bundles is common in, many proteins. The crystal structure of a parallel pentameric coiled coil, constituting the oligomerization domain in the cartilage oligomeric matrix, protein (COMP), was determined at 2.05 angstroms resolution. The same, structure probably occurs in two other extracellular matrix proteins, thrombospondins 3 and 4. Complementary hydrophobic interactions and, conserved disulfide bridges between the alpha helices result in a, thermostable structure with unusual properties. The long hydrophobic axial, pore is filled with water molecules but can also accommodate small apolar, groups. An "ion trap" is formed inside the pore by a ring of conserved, glutamines, which binds chloride and probably other monatomic anions. The, ... [(full description)]
About this Structure
1VDF is a [Single protein] structure of sequence from [Rattus norvegicus] with CL as [ligand]. Structure known Active Site: ION. Full crystallographic information is available from [OCA].
Reference
The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?, Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J, Science. 1996 Nov 1;274(5288):761-5. PMID:8864111
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