1mz9
From Proteopedia
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Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3
Overview
The five-stranded coiled-coil domain of cartilage oligomeric matrix, protein (COMPcc) forms a continuous axial pore with binding capacities for, hydrophobic compounds, including prominent cell signalling molecules., Here, we report the X-ray structure of the COMPcc domain in complex with, vitamin D(3) at 1.7 A resolution. The COMPcc pentamer harbours two, molecules of the steroid hormone precursor in a planar s-trans, conformation of the conjugated triene, with the aliphatic tails lying, along the molecule axis. A hydrophilic ring of five Gln54 side chains, divides the channel into two hydrophobic compartments in which the bound, vitamin D(3) pair is fixed in a head-to-head orientation. Vitamin D(3), binding induces a volumetric increase of the cavities of approximately 30%, while the main chain distances of the pentamer are retained. This, adaptation to the bulky ring systems of the ligands is accomplished by a, rotamer re-orientation of beta-branched side chains that form the knobs, into holes of the coiled-coil structure. Compared with binding of vitamin, D and retinoic acid by their classical receptors, COMP exerts a distinct, mechanism of interaction mainly defined by the pattern of hydrophobic core, residues.
About this Structure
1MZ9 is a Single protein structure of sequence from Mus musculus with VDY as ligand. Full crystallographic information is available from OCA.
Reference
Storage function of cartilage oligomeric matrix protein: the crystal structure of the coiled-coil domain in complex with vitamin D(3)., Ozbek S, Engel J, Stetefeld J, EMBO J. 2002 Nov 15;21(22):5960-8. PMID:12426368
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