1vdf

From Proteopedia

Revision as of 15:13, 5 November 2007

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, oligomerization domain of COMP has marked similarities with proposed, models of the pentameric transmembrane ion channels in phospholamban and, the acetylcholine receptor.

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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