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Article

Analysis by substituted cysteine scanning mutagenesis of the fourth transmembrane domain of the CXCR4 receptor in its inactive and active state.

Biochemical pharmacology - 15 Feb 2013

Boulais Philip E, Escher Emanuel, Leduc Richard

Abstract excerpt

The chemokine SDF-1 (CXCL12) selectively binds to CXCR4, a member of the G protein-coupled receptor (GPCR) superfamily. In this study, we used the substituted-cysteine accessibility method (SCAM) to identify specific residues of the fourth transmembrane domain (TM4) that contribute to the formation of the binding pocket of CXCR4 in its inactive and active state. We successively substituted each residue from...

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Identifiers

PMID: 23219524
DOI: 10.1016/j.bcp.2012.11.022

Genes

CXCR4
CXCL12

Variants

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