2rfa: Difference between revisions
New page: left|200px<br /><applet load="2rfa" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rfa, resolution 1.700Å" /> '''Crystal structure o... |
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'''Crystal structure of the mouse TRPV6 ankyrin repeat domain''' | {{Structure | ||
|PDB= 2rfa |SIZE=350|CAPTION= <scene name='initialview01'>2rfa</scene>, resolution 1.700Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= Trpv6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''Crystal structure of the mouse TRPV6 ankyrin repeat domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2RFA is a [ | 2RFA 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=2RFA OCA]. | ||
==Reference== | ==Reference== | ||
Structural Analyses of the Ankyrin Repeat Domain of TRPV6 and Related TRPV Ion Channels(,)., Phelps CB, Huang RJ, Lishko PV, Wang RR, Gaudet R, Biochemistry. 2008 Feb 26;47(8):2476-84. Epub 2008 Jan 31. PMID:[http:// | Structural Analyses of the Ankyrin Repeat Domain of TRPV6 and Related TRPV Ion Channels(,)., Phelps CB, Huang RJ, Lishko PV, Wang RR, Gaudet R, Biochemistry. 2008 Feb 26;47(8):2476-84. Epub 2008 Jan 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18232717 18232717] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trpv6]] | [[Category: trpv6]] | ||
''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 18:35:31 2008'' | ||
Revision as of 19:35, 20 March 2008
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| , resolution 1.700Å | |||||||
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| Gene: | Trpv6 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the mouse TRPV6 ankyrin repeat domain
OverviewOverview
Transient receptor potential (TRP) proteins are cation channels composed of a transmembrane domain flanked by large N- and C-terminal cytoplasmic domains. All members of the vanilloid family of TRP channels (TRPV) possess an N-terminal ankyrin repeat domain (ARD). The ARD of mammalian TRPV6, an important regulator of calcium uptake and homeostasis, is essential for channel assembly and regulation. The 1.7 A crystal structure of the TRPV6-ARD reveals conserved structural elements unique to the ARDs of TRPV proteins. First, a large twist between the fourth and fifth repeats is induced by residues conserved in all TRPV ARDs. Second, the third finger loop is the most variable region in sequence, length and conformation. In TRPV6, a number of putative regulatory phosphorylation sites map to the base of this third finger. Size exclusion chromatography and crystal packing indicate that the TRPV6-ARD does not assemble as a tetramer and is monomeric in solution. Adenosine triphosphate-agarose and calmodulin-agarose pull-down assays show that the TRPV6-ARD does not interact with either ligand, indicating a different functional role for the TRPV6-ARD than in the paralogous thermosensitive TRPV1 channel. Similar biochemical findings are also presented for the highly homologous mammalian TRPV5-ARD. The implications of the structural and biochemical data on the role of the ankyrin repeats in different TRPV channels are discussed.
About this StructureAbout this Structure
2RFA is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural Analyses of the Ankyrin Repeat Domain of TRPV6 and Related TRPV Ion Channels(,)., Phelps CB, Huang RJ, Lishko PV, Wang RR, Gaudet R, Biochemistry. 2008 Feb 26;47(8):2476-84. Epub 2008 Jan 31. PMID:18232717
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