2CSA

Structure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal

2CSA の概要

• エントリーDOI: 10.2210/pdb2csa/pdb
• 分子名称: Muscarinic acetylcholine receptor M3 (1 entity in total)
• 機能のキーワード: basolateral sorting-signal blss beta-turn, signaling protein-membrane protein complex, signaling protein/membrane protein
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P20309
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1995.02

構造登録者

Iverson, H.A.,Fox, D.,Nadler, L.S.,Klevit, R.E.,Nathanson, N.M. (登録日: 2005-05-21, 公開日: 2005-05-31, 最終更新日: 2024-05-22)

主引用文献

Iverson, H.A.,Fox, D.,Nadler, L.S.,Klevit, R.E.,Nathanson, N.M.
Identification and structural determination of the M3 muscarinic acetylcholine receptor basolateral sorting signal.
J.Biol.Chem., 280:24568-24575, 2005

PubMed Abstract: Muscarinic acetylcholine receptors comprise a family of G-protein-coupled receptors that display differential localization in polarized epithelial cells. We identify a seven-residue sequence, Ala(275)-Val(281), in the third intracellular loop of the M(3) muscarinic receptor that mediates dominant, position-independent basolateral targeting in Madin-Darby canine kidney cells. Mutational analyses identify Glu(276), Phe(280), and Val(281) as critical residues within this sorting motif. Phe(280) and Val(281) comprise a novel dihydrophobic sorting signal as mutations of either residue singly or together with leucine do not disrupt basolateral targeting. Conversely, Glu(276) is required and cannot be substituted with alanine or aspartic acid. A 19-amino acid peptide representing the M(3) sorting signal and surrounding sequence was analyzed via two-dimensional nuclear magnetic resonance spectroscopy. Solution structures show that Glu(276) resides in a type IV beta-turn and the dihydrophobic sequence Phe(280)Val(281) adopts either a type I or IV beta-turn.

PubMed: 15870063
DOI: 10.1074/jbc.M501264200

実験手法

SOLUTION NMR