2N7Q

Structure of the transmembrane domain of human nicastrin in SDS micelles

2N7Q の概要

• エントリーDOI: 10.2210/pdb2n7q/pdb
• 関連するPDBエントリー: 2N7R
• NMR情報: BMRB: 25817
• 分子名称: Nicastrin (1 entity in total)
• 機能のキーワード: detergent micelles, gamma-secretase, nicastrin, membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane ; Single-pass type I membrane protein : Q92542
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5992.00

構造登録者

Li, Y.,Liew, L.,Li, Q.,Kang, C. (登録日: 2015-09-17, 公開日: 2016-04-27, 最終更新日: 2024-05-01)

主引用文献

Li, Y.,Liew, L.S.,Li, Q.,Kang, C.
Structure of the transmembrane domain of human nicastrin-a component of gamma-secretase
Sci Rep, 6:19522-19522, 2016

PubMed Abstract: Nicastrin is the largest component of γ-secretase that is an intramembrane protease important in the development of Alzheimer's disease. Nicastrin contains a large extracellular domain, a single transmembrane (TM) domain, and a short C-terminus. Its TM domain is important for the γ-secretase complex formation. Here we report nuclear magnetic resonance (NMR) studies of the TM and C-terminal regions of human nicastrin in both sodium dodecyl sulfate (SDS) and dodecylphosphocholine (DPC) micelles. Structural study and dynamic analysis reveal that the TM domain is largely helical and stable under both SDS and DPC micelles with its N-terminal region undergoing intermediate time scale motion. The TM helix contains a hydrophilic patch that is important for TM-TM interactions. The short C-terminus is not structured in solution and a region formed by residues V697-A702 interacts with the membrane, suggesting that these residues may play a role in the γ-secretase complex formation. Our study provides structural insight into the function of the nicastrin TM domain and the C-terminus in γ-secretase complex.

PubMed: 26776682
DOI: 10.1038/srep19522

実験手法

SOLUTION NMR