2ETC

Crystal structure of the ankyrin repeat domain of TRPV2

2ETC の概要

• エントリーDOI: 10.2210/pdb2etc/pdb
• 関連するPDBエントリー: 2ET9 2ETA 2ETB
• 分子名称: Transient receptor potential cation channel subfamily V member 2 (1 entity in total)
• 機能のキーワード: trpv2, ankyrin repeat domain, transport protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q9WUD2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61147.56

構造登録者

Jin, X.,Gaudet, R. (登録日: 2005-10-27, 公開日: 2006-06-27, 最終更新日: 2024-11-20)

主引用文献

Jin, X.,Touhey, J.,Gaudet, R.
Structure of the N-terminal Ankyrin Repeat Domain of the TRPV2 Ion Channel.
J.Biol.Chem., 281:25006-25010, 2006

PubMed Abstract: The TRPV ion channels mediate responses to many sensory stimuli including heat, low pH, neuropeptides, and chemical ligands. All TRPV subfamily members contain an intracellular N-terminal ankyrin repeat domain (ARD), a prevalent protein interaction motif. The 1.6-A crystal structure of the TRPV2-ARD, with six ankyrin repeats, reveals several atypical structural features. Repeats one through three display unusually long and flexible fingers with a large number of exposed aromatic residues, whereas repeats five and six have unusually long outer helices. Furthermore, a large counterclockwise twist observed in the stacking of repeats four and five breaks the regularity of the domain, altering the shape of surfaces available for interactions with proteins or other cellular ligands. Both solution studies and crystal packing interactions indicate that the TRPV2-ARD does not form homo-oligomers, suggesting that the ARD of TRPV ion channels may be used for interactions with regulatory factors rather than in promoting tetrameric assembly of the ion channels.

PubMed: 16809337
DOI: 10.1074/jbc.C600153200

実験手法

X-RAY DIFFRACTION (3.1 Å)