2JXO

Structure of the second PDZ domain of NHERF-1

2JXO の概要

• エントリーDOI: 10.2210/pdb2jxo/pdb
• NMR情報: BMRB: 15567
• 分子名称: Ezrin-radixin-moesin-binding phosphoprotein 50 (1 entity in total)
• 機能のキーワード: nherf-1, pdz domain, pdz2, acetylation, cell projection, membrane, phosphoprotein, polymorphism, wnt signaling pathway, protein binding
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm (By similarity): O14745
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10725.14

構造登録者

Cheng, H.,Li, J.,Dai, Z.,Bu, Z.,Roder, H. (登録日: 2007-11-27, 公開日: 2008-12-09, 最終更新日: 2024-05-29)

主引用文献

Cheng, H.,Li, J.,Fazlieva, R.,Dai, Z.,Bu, Z.,Roder, H.
Autoinhibitory Interactions between the PDZ2 and C-terminal Domains in the Scaffolding Protein NHERF1
Structure, 17:660-669, 2009

PubMed Abstract: Na(+)/H(+) exchanger regulatory factor (NHERF1) is a signaling adaptor protein comprising two PDZ domains and a C-terminal ezrin-binding (EB) motif. To understand the role of intramolecular interactions in regulating its binding properties, we characterized the complex between the second PDZ domain PDZ2 and the C-terminal 242-358 fragment of NHERF1 using NMR and fluorescence methods. NMR chemical shift and relaxation data implicate 11 C-terminal residues in binding and, together with a thermodynamic analysis of mutant proteins, indicate that the EB region becomes helical when bound to PDZ2. Both specific contacts between PDZ2 and EB as well as nonspecific interactions involving a 100-residue flexible linker contribute to stabilizing two structurally distinct closed conformations of NHERF1. The affinity of mutant proteins for an extrinsic ligand is inversely related to the helix-forming propensity of the EB motif. The findings provide a structural framework for understanding how autoinhibitory interactions modulated the binding properties of NHERF1.

PubMed: 19446522
DOI: 10.1016/j.str.2009.03.009

実験手法

SOLUTION NMR