2ELB

Crystal Structure of the BAR-PH domain of human APPL1

2ELB の概要

• エントリーDOI: 10.2210/pdb2elb/pdb
• 関連するPDBエントリー: 2ELA
• 分子名称: Adapter protein containing PH domain, PTB domain and leucine zipper motif 1 (1 entity in total)
• 機能のキーワード: appl, bar domain, ph domain, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Early endosome membrane; Peripheral membrane protein: Q9UKG1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45987.12

構造登録者

Li, J.,Mao, X.,Dong, L.Q.,Liu, F.,Tong, L. (登録日: 2007-03-27, 公開日: 2007-05-29, 最終更新日: 2024-11-06)

主引用文献

Li, J.,Mao, X.,Dong, L.Q.,Liu, F.,Tong, L.
Crystal Structures of the BAR-PH and PTB Domains of Human APPL1
Structure, 15:525-533, 2007

PubMed Abstract: APPL1 interacts with adiponectin receptors and other important signaling molecules. It contains a BAR and a PH domain near its N terminus, and the two domains may function as a unit (BAR-PH domain). We report here the crystal structures of the BAR-PH and PTB domains of human APPL1. The structures reveal novel features for BAR domain dimerization and for the interactions between the BAR and PH domains. The BAR domain dimer of APPL1 contains two four-helical bundles, whereas other BAR domain dimers have only three helices in each bundle. The PH domain is located at the opposite ends of the BAR domain dimer. Yeast two-hybrid assays confirm the interactions between the BAR and PH domains. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. The ability of APPL1 to interact with multiple signaling molecules and phospholipids supports an important role for this adaptor in cell signaling.

PubMed: 17502098
DOI: 10.1016/j.str.2007.03.011

実験手法

X-RAY DIFFRACTION (2.6 Å)