Abstract
Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.
Highlights
Sorting nexin 3 (SNX3) belongs to a subfamily of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes
We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini
The SNX3 protein is localized within the early endosome through its interaction with phosphatidylinositol 3-phosphate (PI3P) (Xu et al 2001)
Summary
The SNX3 protein is localized within the early endosome through its interaction with phosphatidylinositol 3-phosphate (PI3P) (Xu et al 2001). It associates with the cargo-selective retromer complex VPS26-VPS29-VPS35 in a trafficking pathway, forming a retromer capable of transporting Wntless from the endosome to the trans-Golgi network (Harterink et al 2011). PX domain-containing proteins are well known for their phosphatidylinositide binding activities, and are typically 120 amino acids in length. Their structural domains typically contain three antiparallel b strands followed by an unstructured loop with a conserved PXXP motif followed by three a helices. The assignment of the resonances provides a basis for the structural and dynamic analysis of this full length protein and its ligand and membrane binding mechanisms
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