2rfa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2rfa.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2rfa.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rfa| PDB=2rfa | SCENE= }}
{{STRUCTURE_2rfa| PDB=2rfa | SCENE= }}
-
'''Crystal structure of the mouse TRPV6 ankyrin repeat domain'''
+
===Crystal structure of the mouse TRPV6 ankyrin repeat domain===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18232717}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18232717 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18232717}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Transport]]
[[Category: Transport]]
[[Category: Trpv6]]
[[Category: Trpv6]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:47:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:08:39 2008''

Revision as of 03:08, 28 July 2008

Image:2rfa.png

Template:STRUCTURE 2rfa

Crystal structure of the mouse TRPV6 ankyrin repeat domain

Template:ABSTRACT PUBMED 18232717

About this Structure

2RFA is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

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:18232717

Page seeded by OCA on Mon Jul 28 06:08:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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