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Dynamic structure of the full-length scaffolding protein NHERF1 influences signaling complex assembly.

J. Biol. Chem.. 2019; 
BhattacharyaShibani,StanleyChristopher B,HellerWilliam T,FriedmanPeter A,BuZ
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Peptide Synthesis The 22-residue C-ter- Structure of wildtype NHERF1 and disease variants minal peptide from GRK6A with an N-terminal biotin tag was custom synthesized (Genscript, NJ). Get A Quote

Abstract

The Na/H exchange regulatory cofactor 1 (NHERF1) protein modulates the assembly and intracellular trafficking of several transmembrane G protein-coupled receptors (GPCRs) and ion transport proteins with the membrane-cytoskeleton adapter protein ezrin. Here, we applied solution NMR and small-angle neutron scattering (SANS) to structurally characterize full-length NHERF1 and disease-associated variants that are implicated in impaired phosphate homeostasis. Using NMR, we mapped the modular architecture of NHERF1, which is composed of two structurally-independent PDZ domains that are connected by a flexible, disordered linker. We observed that the ultra-long and disordered C-terminal tail of NHERF1 has a ty... More

Keywords

GRK6A,NHERF1,PDZ domain,ezrin,neutron scattering,nuclear magnetic resonance (NMR),scaffold pro