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1vdf

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Revision as of 10:02, 8 January 2020

ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN

Structural highlights

1vdf is a 5 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COMP_RAT] May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (By similarity). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Oligomerization by the formation of alpha-helical bundles is common in many proteins. The crystal structure of a parallel pentameric coiled coil, constituting the oligomerization domain in the cartilage oligomeric matrix protein (COMP), was determined at 2.05 angstroms resolution. The same structure probably occurs in two other extracellular matrix proteins, thrombospondins 3 and 4. Complementary hydrophobic interactions and conserved disulfide bridges between the alpha helices result in a thermostable structure with unusual properties. The long hydrophobic axial pore is filled with water molecules but can also accommodate small apolar groups. An "ion trap" is formed inside the pore by a ring of conserved glutamines, which binds chloride and probably other monatomic anions. The oligomerization domain of COMP has marked similarities with proposed models of the pentameric transmembrane ion channels in phospholamban and the acetylcholine receptor.

The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?,Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J Science. 1996 Nov 1;274(5288):761-5. PMID:8864111^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J. The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel? Science. 1996 Nov 1;274(5288):761-5. PMID:8864111

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vdf"

@@ Line 1: / Line 1: @@
 ==ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN==
-<StructureSection load='1vdf' size='340' side='right' caption='[[1vdf]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+<StructureSection load='1vdf' size='340' side='right'caption='[[1vdf]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1vdf]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VDF FirstGlance]. <br>
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Buffalo rat]]
+[[Category: Large Structures]]
 [[Category: Malashkevich, V N]]
 [[Category: Assembly domain]]

1vdf

From Proteopedia

Revision as of 10:02, 8 January 2020

ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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