4CMZ

An intertwined homodimer of the PDZ homology domain of periaxin

4CMZ の概要

• エントリーDOI: 10.2210/pdb4cmz/pdb
• 分子名称: PERIAXIN (2 entities in total)
• 機能のキーワード: cell cycle, domain swapping, intertwining
• 由来する生物種: Homo sapiens (HUMAN)
• 細胞内の位置: Isoform 1: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Isoform 2: Cytoplasm . Cell membrane : Q9BXM0
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 30135.88

構造登録者

Han, H.,Kursula, P. (登録日: 2014-01-20, 公開日: 2014-04-02, 最終更新日: 2024-05-08)

主引用文献

Han, H.,Kursula, P.
Periaxin and Ahnak Nucleoprotein 2 Form Intertwined Homodimers Through Domain Swapping
J.Biol.Chem., 289:14121-, 2014

PubMed Abstract: Periaxin (PRX) is an abundant protein in the peripheral nervous system, with an important role in myelination. PRX participates in large molecular complexes, most likely through the interactions of its N-terminal PSD-95/Discs-large/ZO-1 (PDZ)-like domain. We present the crystal structures of the PDZ-like domains from PRX and its homologue AHNAK nucleoprotein 2 (AHNAK2). The unique intertwined, domain-swapped dimers provide a structural basis for the homodimerization of both proteins. The core of the homodimer is formed by a 6-stranded antiparallel β sheet, with every other strand from a different chain. The AHNAK2 PDZ domain structure contains a bound class III ligand peptide. The binding pocket is preformed, and the peptide-PDZ interactions have unique aspects, including two salt bridges and weak recognition of the peptide C terminus. Tight homodimerization may be central to the scaffolding functions of PRX and AHNAK2 in molecular complexes linking the extracellular matrix to the cytoskeletal network.

PubMed: 24675079
DOI: 10.1074/JBC.M114.554816

実験手法

X-RAY DIFFRACTION (2.7 Å)