1mz9: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 17: | Line 26: | ||
[[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 13:50, 20 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3
OverviewOverview
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 StructureAbout this Structure
1MZ9 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Mar 20 12:50:03 2008