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6N5Z

Crystal structure of the SNX5 PX domain in complex with the Sema4C

Summary for 6N5Z
Entry DOI10.2210/pdb6n5z/pdb
DescriptorSorting nexin-5,Semaphorin-4C, CHLORIDE ION (3 entities in total)
Functional Keywordssorting nexin, snx, endosome, endocytosis
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight40654.96
Authors
Collins, B.,Paul, B.,Weeratunga, S. (deposition date: 2018-11-22, release date: 2019-09-18, Last modification date: 2024-03-13)
Primary citationSimonetti, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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