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• W2023555945 abstract "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." @default.
• W2023555945 created "2016-06-24" @default.
• W2023555945 creator A5012954903 @default.
• W2023555945 creator A5076921484 @default.
• W2023555945 creator A5078791008 @default.
• W2023555945 date "2002-11-15" @default.
• W2023555945 modified "2023-10-14" @default.
• W2023555945 title "Storage function of cartilage oligomeric matrix protein: the crystal structure of the coiled-coil domain in complex with vitamin D3" @default.
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• W2023555945 doi "https://doi.org/10.1093/emboj/cdf628" @default.
• W2023555945 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/137217" @default.
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