2RFA

Crystal structure of the mouse TRPV6 ankyrin repeat domain

2RFA の概要

• エントリーDOI: 10.2210/pdb2rfa/pdb
• 分子名称: Transient receptor potential cation channel subfamily V member 6 (2 entities in total)
• 機能のキーワード: trpv6, ankyrin reapeat, transient receptor potential, ank repeat, calcium channel, calcium transport, calmodulin-binding, glycoprotein, ion transport, ionic channel, membrane, transmembrane, transport, membrane protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell membrane ; Multi- pass membrane protein : Q91WD2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25707.59

構造登録者

Phelps, C.B.,Huang, R.J.,Wang, R.R.,Gaudet, R. (登録日: 2007-09-28, 公開日: 2008-02-19, 最終更新日: 2024-02-21)

主引用文献

Phelps, C.B.,Huang, R.J.,Lishko, P.V.,Wang, R.R.,Gaudet, R.
Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels.
Biochemistry, 47:2476-2484, 2008

PubMed Abstract: 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.

PubMed: 18232717
DOI: 10.1021/bi702109w

実験手法

X-RAY DIFFRACTION (1.7 Å)