1vdf

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[[Image:1vdf.gif|left|200px]]
[[Image:1vdf.gif|left|200px]]
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{{Structure
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|PDB= 1vdf |SIZE=350|CAPTION= <scene name='initialview01'>1vdf</scene>, resolution 2.05&Aring;
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The line below this paragraph, containing "STRUCTURE_1vdf", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=ION:Binds+Cl-'>ION</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1vdf| PDB=1vdf | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vdf OCA], [http://www.ebi.ac.uk/pdbsum/1vdf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vdf RCSB]</span>
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}}
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'''ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN'''
'''ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
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[[Category: assembly domain]]
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[[Category: Assembly domain]]
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[[Category: cartilage]]
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[[Category: Cartilage]]
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[[Category: extracellular matrix protein]]
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[[Category: Extracellular matrix protein]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: oligomeric matrix protein]]
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[[Category: Oligomeric matrix protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:24:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:22:50 2008''
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Revision as of 09:24, 3 May 2008

Template:STRUCTURE 1vdf

ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN


Overview

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.

About this Structure

1VDF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 12:24:29 2008

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