5ELQ

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

Summary for 5ELQ

• Entry DOI: 10.2210/pdb5elq/pdb
• Related: 4Z8J 5EM9 5EMA 5EMB
• Descriptor: Sorting nexin-27, GLU-ASP-GLN-GLU-THR-ALA-VAL, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: endosome, pdz domain, sorting nexin, protein transport
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 4
• Total formula weight: 23812.74

Authors

Collins, B.M.,Clairfeuille, T. (deposition date: 2015-11-05, release date: 2016-09-07, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.1 Å)