6BV7
NMR structure of Sodium/Calcium Exchanger 1 (NCX1) Two-helix Bundle (THB) domain
6BV7 の概要
| エントリーDOI | 10.2210/pdb6bv7/pdb |
| NMR情報 | BMRB: 30379 |
| 分子名称 | Sodium/calcium exchanger 1 (1 entity in total) |
| 機能のキーワード | two-helix bundle, membrane protein |
| 由来する生物種 | Canis lupus familiaris (Dog) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 6788.54 |
| 構造登録者 | |
| 主引用文献 | Yuan, J.,Yuan, C.,Xie, M.,Yu, L.,Bruschweiler-Li, L.,Bruschweiler, R. The Intracellular Loop of the Na+/Ca2+Exchanger Contains an "Awareness Ribbon"-Shaped Two-Helix Bundle Domain. Biochemistry, 57:5096-5104, 2018 Cited by PubMed Abstract: The Na/Ca exchanger (NCX) is a ubiquitous single-chain membrane protein that plays a major role in regulating the intracellular Ca homeostasis by the counter transport of Na and Ca across the cell membrane. Other than its prokaryotic counterpart, which contains only the transmembrane domain and is self-sufficient as an active ion transporter, the eukaryotic NCX protein possesses in addition a large intracellular loop that senses intracellular calcium signals and controls the activation of ion transport across the membrane. This provides a necessary layer of regulation for the more complex function of eukaryotic cells. The Ca sensor in the intracellular loop is known as the Ca-binding domain (CBD12). However, how the signaling of the allosteric intracellular Ca binding propagates and results in transmembrane ion transportation still lacks a detailed explanation. Further structural and dynamics characterization of the intracellular loop flanking both sides of CBD12 is therefore imperative. Here, we report the identification and characterization of another structured domain that is N-terminal to CBD12 in the intracellular loop using solution nuclear magnetic resonance (NMR) spectroscopy. The atomistic structure of this domain reveals that two tandem long α-helices, connected by a short linker, form a stable crossover two-helix bundle (THB), resembling an "awareness ribbon". Considering the highly conserved amino acid sequence of the THB domain, the detailed structural and dynamics properties of the THB domain will be common among NCXs from different species and will contribute toward the understanding of the regulatory mechanism of eukaryotic Na/Ca exchangers. PubMed: 29898361DOI: 10.1021/acs.biochem.8b00300 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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