Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4RDQ

Calcium-activated chloride channel bestrophin-1, from chicken, in complex with Fab antibody fragments, chloride and calcium

4RDQ の概要
エントリーDOI10.2210/pdb4rdq/pdb
分子名称Bestrophin-1, Fab antibody fragment, light chain, Fab antibody fragment, heavy chain, ... (9 entities in total)
機能のキーワードtransmembrane protein, membrane protein, ion channel, calcium-activated chloride channel, cacc, anion channel, membrane, transport protein
由来する生物種Gallus gallus (bantam,chickens)
詳細
タンパク質・核酸の鎖数15
化学式量合計479356.81
構造登録者
Dickson, V.K.,Pedi, L.,Long, S.B. (登録日: 2014-09-19, 公開日: 2014-10-22, 最終更新日: 2024-11-20)
主引用文献Kane Dickson, V.,Pedi, L.,Long, S.B.
Structure and insights into the function of a Ca(2+)-activated Cl(-) channel.
Nature, 516:213-218, 2014
Cited by
PubMed Abstract: Bestrophin calcium-activated chloride channels (CaCCs) regulate the flow of chloride and other monovalent anions across cellular membranes in response to intracellular calcium (Ca(2+)) levels. Mutations in bestrophin 1 (BEST1) cause certain eye diseases. Here we present X-ray structures of chicken BEST1-Fab complexes, at 2.85 Å resolution, with permeant anions and Ca(2+). Representing, to our knowledge, the first structure of a CaCC, the eukaryotic BEST1 channel, which recapitulates CaCC function in liposomes, is formed from a pentameric assembly of subunits. Ca(2+) binds to the channel's large cytosolic region. A single ion pore, approximately 95 Å in length, is located along the central axis and contains at least 15 binding sites for anions. A hydrophobic neck within the pore probably forms the gate. Phenylalanine residues within it may coordinate permeating anions via anion-π interactions. Conformational changes observed near the 'Ca(2+) clasp' hint at the mechanism of Ca(2+)-dependent gating. Disease-causing mutations are prevalent within the gating apparatus.
PubMed: 25337878
DOI: 10.1038/nature13913
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.85 Å)
構造検証レポート
Validation report summary of 4rdq
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

PDB statisticsPDBj update infoContact PDBjnumon