6N5X

Crystal structure of the SNX5 PX domain in complex with the CI-MPR (space group P212121 - Form 1)

6N5X の概要

• エントリーDOI: 10.2210/pdb6n5x/pdb
• 分子名称: Sorting nexin-5,Cation-independent mannose-6-phosphate receptor, GLYCEROL, O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500), ... (4 entities in total)
• 機能のキーワード: sorting nexin, snx, endosome, endocytosis
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21714.33

構造登録者

Collins, B.,Paul, B.,Weeratunga, S. (登録日: 2018-11-22, 公開日: 2019-09-18, 最終更新日: 2024-03-13)

主引用文献

Simonetti, B.,Paul, B.,Chaudhari, K.,Weeratunga, S.,Steinberg, F.,Gorla, M.,Heesom, K.J.,Bashaw, G.J.,Collins, B.M.,Cullen, P.J.
Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins.
Nat.Cell Biol., 21:1219-1233, 2019

PubMed Abstract: Protein trafficking requires coat complexes that couple recognition of sorting motifs in transmembrane cargoes with biogenesis of transport carriers. The mechanisms of cargo transport through the endosomal network are poorly understood. Here, we identify a sorting motif for endosomal recycling of cargoes, including the cation-independent mannose-6-phosphate receptor and semaphorin 4C, by the membrane tubulating BAR domain-containing sorting nexins SNX5 and SNX6. Crystal structures establish that this motif folds into a β-hairpin, which binds a site in the SNX5/SNX6 phox homology domains. Over sixty cargoes share this motif and require SNX5/SNX6 for their recycling. These include cargoes involved in neuronal migration and a Drosophila snx6 mutant displays defects in axonal guidance. These studies identify a sorting motif and provide molecular insight into an evolutionary conserved coat complex, the 'Endosomal SNX-BAR sorting complex for promoting exit 1' (ESCPE-1), which couples sorting motif recognition to the BAR-domain-mediated biogenesis of cargo-enriched tubulo-vesicular transport carriers.

PubMed: 31576058
DOI: 10.1038/s41556-019-0393-3

実験手法

X-RAY DIFFRACTION (2.051 Å)