1mz9: Difference between revisions

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[[Image:1mz9.jpg|left|200px]]
{{Seed}}
[[Image:1mz9.png|left|200px]]


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{{STRUCTURE_1mz9|  PDB=1mz9  |  SCENE=  }}  
{{STRUCTURE_1mz9|  PDB=1mz9  |  SCENE=  }}  


'''Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3'''
===Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12426368}}


==About this Structure==
==About this Structure==
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[[Category: Stetefeld, J.]]
[[Category: Stetefeld, J.]]
[[Category: Pentameric coiled-coil domain]]
[[Category: Pentameric coiled-coil domain]]
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