1mz9

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[[Image:1mz9.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1mz9", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=VDY:3-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANOL'>VDY</scene>
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{{STRUCTURE_1mz9| PDB=1mz9 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mz9 OCA], [http://www.ebi.ac.uk/pdbsum/1mz9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mz9 RCSB]</span>
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'''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'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Stetefeld, J.]]
[[Category: Stetefeld, J.]]
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[[Category: pentameric coiled-coil domain]]
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[[Category: Pentameric coiled-coil domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:53:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:23:09 2008''
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Revision as of 22:53, 2 May 2008

Template:STRUCTURE 1mz9

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. 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 Page seeded by OCA on Sat May 3 01:53:22 2008

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