5EMA

Crystal structure of the SNX27 PDZ domain bound to the phosphorylated C-terminal LRRC3B PDZ binding motif

5EMA の概要

• エントリーDOI: 10.2210/pdb5ema/pdb
• 関連するPDBエントリー: 4Z8J 5ELQ 5EM9 5EMB
• 分子名称: Sorting nexin-27, ASP-ASP-ILE-SEP-THR-VAL-VAL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: endosome, pdz domain, sorting nexin, protein transport
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11586.93

構造登録者

Collins, B.M.,Clairfeuille, T. (登録日: 2015-11-06, 公開日: 2016-09-07, 最終更新日: 2024-11-13)

主引用文献

Clairfeuille, T.,Mas, C.,Chan, A.S.,Yang, Z.,Tello-Lafoz, M.,Chandra, M.,Widagdo, J.,Kerr, M.C.,Paul, B.,Merida, I.,Teasdale, R.D.,Pavlos, N.J.,Anggono, V.,Collins, B.M.
A molecular code for endosomal recycling of phosphorylated cargos by the SNX27-retromer complex.
Nat.Struct.Mol.Biol., 23:921-932, 2016

PubMed Abstract: Recycling of internalized receptors from endosomal compartments is essential for the receptors' cell-surface homeostasis. Sorting nexin 27 (SNX27) cooperates with the retromer complex in the recycling of proteins containing type I PSD95-Dlg-ZO1 (PDZ)-binding motifs. Here we define specific acidic amino acid sequences upstream of the PDZ-binding motif required for high-affinity engagement of the human SNX27 PDZ domain. However, a subset of SNX27 ligands, such as the β adrenergic receptor and N-methyl-D-aspartate (NMDA) receptor, lack these sequence determinants. Instead, we identified conserved sites of phosphorylation that substitute for acidic residues and dramatically enhance SNX27 interactions. This newly identified mechanism suggests a likely regulatory switch for PDZ interaction and protein transport by the SNX27-retromer complex. Defining this SNX27 binding code allowed us to classify more than 400 potential SNX27 ligands with broad functional implications in signal transduction, neuronal plasticity and metabolite transport.

PubMed: 27595347
DOI: 10.1038/nsmb.3290

実験手法

X-RAY DIFFRACTION (1.32 Å)