1mz9
From Proteopedia
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- | [[Image:1mz9.jpg|left|200px]] | + | [[Image:1mz9.jpg|left|200px]] |
- | + | ||
- | '''Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3''' | + | {{Structure |
+ | |PDB= 1mz9 |SIZE=350|CAPTION= <scene name='initialview01'>1mz9</scene>, resolution 1.70Å | ||
+ | |SITE= | ||
+ | |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> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1MZ9 is a [ | + | 1MZ9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZ9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12426368 12426368] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pentameric coiled-coil domain]] | [[Category: pentameric coiled-coil domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:50:03 2008'' |
Revision as of 10:50, 20 March 2008
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, resolution 1.70Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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
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