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Updated: Apr 14, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Secondary structure and (1)H, (13)C, (15)N resonance assignments of the endosomal sorting protein sorting nexin 3
Michael Overduin1, Sandya Rajesh1, Jean Gruenberg2
1Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
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 (1)H, (13)C and (15)N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.
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