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2rfa

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Revision as of 01:38, 25 December 2014

Crystal structure of the mouse TRPV6 ankyrin repeat domain

Structural highlights

2rfa is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Trpv6 (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TRPV6_MOUSE] Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.^[1] ^[2]

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

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.

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^[3]

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

References

↑ Voets T, Janssens A, Prenen J, Droogmans G, Nilius B. Mg2+-dependent gating and strong inward rectification of the cation channel TRPV6. J Gen Physiol. 2003 Mar;121(3):245-60. PMID:12601087
↑ Hoenderop JG, Voets T, Hoefs S, Weidema F, Prenen J, Nilius B, Bindels RJ. Homo- and heterotetrameric architecture of the epithelial Ca2+ channels TRPV5 and TRPV6. EMBO J. 2003 Feb 17;22(4):776-85. PMID:12574114 doi:http://dx.doi.org/10.1093/emboj/cdg080
↑ Phelps CB, Huang RJ, Lishko PV, Wang RR, Gaudet R. Structural Analyses of the Ankyrin Repeat Domain of TRPV6 and Related TRPV Ion Channels(,). Biochemistry. 2008 Feb 26;47(8):2476-84. Epub 2008 Jan 31. PMID:18232717 doi:10.1021/bi702109w

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rfa"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2rfa]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RFA FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trpv6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trpv6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rfa RCSB], [http://www.ebi.ac.uk/pdbsum/2rfa PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rfa RCSB], [http://www.ebi.ac.uk/pdbsum/2rfa PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TRPV6_MOUSE TRPV6_MOUSE]] Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.<ref>PMID:12601087</ref> <ref>PMID:12574114</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 34: @@
 </StructureSection>
 [[Category: Mus musculus]]
-[[Category: Gaudet, R.]]
+[[Category: Gaudet, R]]
-[[Category: Huang, R J.]]
+[[Category: Huang, R J]]
-[[Category: Phelps, C B.]]
+[[Category: Phelps, C B]]
-[[Category: Wang, R R.]]
+[[Category: Wang, R R]]
 [[Category: Ank repeat]]
 [[Category: Ankyrin reapeat]]

2rfa

From Proteopedia

Revision as of 01:38, 25 December 2014

Crystal structure of the mouse TRPV6 ankyrin repeat domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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