1VRY

Second and Third Transmembrane Domains of the Alpha-1 Subunit of Human Glycine Receptor

「1ZHD」から置き換えられました

1VRY の概要

• エントリーDOI: 10.2210/pdb1vry/pdb
• 分子名称: Glycine receptor alpha-1 chain (1 entity in total)
• 機能のキーワード: glycine receptor, second transmembrane domain, third transmembrane domain, membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P23415
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8530.07

構造登録者

Ma, D.,Liu, Z.,Li, L.,Tang, P.,Xu, Y. (登録日: 2005-07-20, 公開日: 2005-07-26, 最終更新日: 2023-12-27)

主引用文献

Ma, D.,Liu, Z.,Li, L.,Tang, P.,Xu, Y.
Structure and Dynamics of the Second and Third Transmembrane Domains of Human Glycine Receptor.
Biochemistry, 44:8790-8800, 2005

PubMed Abstract: A 61-residue polypeptide resembling the second and third transmembrane domains (TM23) of the alpha-1 subunit of human glycine receptor and its truncated form, both with the wild-type loop linking the two TM domains (the "23" loop), were studied using high-resolution NMR. Well-defined domain structures can be identified for the TM2, 23 loop, and TM3 regions. Contrary to the popular model of a long and straight alpha-helical structure for the pore-lining TM2 domain for the Cys-loop receptor family, the last three residues of the TM2 domain and the first eight residues of the 23 loop (S16-S26) seem to be intrinsically nonhelical and highly flexible even in trifluoroethanol, a solvent known to promote and stabilize alpha-helical structures. The six remaining residues of the 23 loop and most of the TM3 domain exhibit helical structures with a kinked pi-helix (or a pi-turn) from W34 to C38 and a kink angle of 159 +/- 3 degrees . The tertiary fold of TM3 relative to TM2 is defined by several unambiguously identified long-range NOE cross-peaks within the loop region and between TM2 and TM3 domains. The 20 lowest-energy structures show a left-handed tilt of TM3 relative to TM2 with a tilting angle of 44 +/- 2 degrees between TM2 (V1-Q14) and TM3 (L39-E48) helix axes. This left-handed TM2-TM3 arrangement ensures a neatly packed right-handed quaternary structure of five subunits to form an ion-conducting pore. This is the first time that two TM domains of the glycine receptor linked by the important 23 loop have ever been analyzed at atomistic resolution. Many structural characteristics of the receptor can be inferred from the structural and dynamical features identified in this study.

PubMed: 15952785
DOI: 10.1021/bi050256n

実験手法

SOLUTION NMR