1mz9: Difference between revisions

Revision as of 00:21, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mz9.png

Template:STRUCTURE 1mz9

Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3Storage function of COMP:the crystal structure of the coiled-coil domain in complex with vitamin D3

Template:ABSTRACT PUBMED 12426368

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 Mon Jul 28 00:21:55 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1mz9.jpg|left|200px]]
+{{Seed}}
+[[Image:1mz9.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{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==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12426368}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12426368 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12426368}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Stetefeld, J.]]
 [[Category: Pentameric coiled-coil domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:53:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:21:55 2008''