3GUA
Sulfates bound in the vestibule of AChBP
3GUA の概要
| エントリーDOI | 10.2210/pdb3gua/pdb |
| 分子名称 | Soluble acetylcholine receptor, SULFATE ION (3 entities in total) |
| 機能のキーワード | ion channel, ion selectivity, ion filter, receptor, choline-binding protein |
| 由来する生物種 | Aplysia californica (California sea hare) |
| タンパク質・核酸の鎖数 | 10 |
| 化学式量合計 | 249292.16 |
| 構造登録者 | |
| 主引用文献 | Hansen, S.B.,Wang, H.L.,Taylor, P.,Sine, S.M. An Ion Selectivity Filter in the Extracellular Domain of Cys-loop Receptors Reveals Determinants for Ion Conductance J.Biol.Chem., 283:36066-36070, 2008 Cited by PubMed Abstract: Neurotransmitter binding to Cys-loop receptors promotes a prodigious transmembrane flux of several million ions/s, but to date, structural determinants of ion flux have been identified flanking the membrane-spanning region. Using x-ray crystallography, sequence analysis, and single-channel recording, we identified a novel determinant of ion conductance near the point of entry of permeant ions. Co-crystallization of acetylcholine-binding protein with sulfate anions revealed coordination of SO4(2-) with a ring of lysines at a position equivalent to 24 A above the lipid membrane in homologous Cys-loop receptors. Analysis of multiple sequence alignments revealed that residues equivalent to the ring of lysines are negatively charged in cation-selective receptors but are positively charged in anion-selective receptors. Charge reversal of side chains at homologous positions in the nicotinic receptor from the motor end plate decreases unitary conductance up to 80%. Selectivity filters stemming from transmembrane alpha-helices have similar pore diameters and compositions of amino acids. These findings establish that when the channel opens under a physiological electrochemical gradient, permeant ions are initially stabilized within the extracellular vestibule of Cys-loop receptors, and this stabilization is a major determinant of ion conductance. PubMed: 18940802DOI: 10.1074/jbc.C800194200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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