1vdf
From Proteopedia
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| - | [[Image:1vdf.gif|left|200px]]<br /><applet load="1vdf" size=" | + | [[Image:1vdf.gif|left|200px]]<br /><applet load="1vdf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vdf, resolution 2.05Å" /> | caption="1vdf, resolution 2.05Å" /> | ||
'''ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN'''<br /> | '''ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=ION:Binds Cl-'>ION</scene>. Full crystallographic information is available from [http:// | + | 1VDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=ION:Binds+Cl-'>ION</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oligomeric matrix protein]] | [[Category: oligomeric matrix protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:16:54 2008'' |
Revision as of 08:16, 3 February 2008
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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 with as ligand. Known structural/functional Site: . 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
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