2JSN

Solution structure of the atypical PDZ-like domain of synbindin

2JSN の概要

• エントリーDOI: 10.2210/pdb2jsn/pdb
• NMR情報: BMRB: 15370
• 分子名称: Trafficking protein particle complex subunit 4 (1 entity in total)
• 機能のキーワード: protein interaction, protein transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10820.21

構造登録者

Feng, Y.,Fan, S.,Gong, W.,Xia, B. (登録日: 2007-07-10, 公開日: 2008-07-15, 最終更新日: 2024-05-08)

主引用文献

Fan, S.,Feng, Y.,Wei, Z.,Xia, B.,Gong, W.
Solution structure of synbindin atypical PDZ domain and interaction with syndecan-2
PROTEIN AND PEPTIDE LETTERS, 16:189-195, 2009

PubMed Abstract: Synbindin is one component of Transport protein particle (TRAPP) complexes. In the hippocampal neurons, synbindin binds syndecan-2 by its atypical PDZ domain (APD) and may regulate the formation of dendritic spines. To investigate the interaction of synbindin and syndecan-2, we determined the solution structure of the synbindin APD by NMR. The structure of APD is different from the classical canonical PDZ domains by lacking the typical alphaA helix and the signature sequence Gly-Psi-Gly-Psi. These differences indicate that APD may not bind syndecan-2 with the typical binding mode of other PDZ domain proteins. In NMR titration experiments, APD do not bind with the C-terminal TKEFYA peptide of syndecan-2, but can interact with the 32-residue cytoplasmic domain of syndecan-2 very weakly.

PubMed: 19200043

実験手法

SOLUTION NMR