Title : Comparative analysis of homology models of the AH receptor ligand binding domain: verification of structure-function predictions by site-directed mutagenesis of a nonfunctional receptor.

Pub. Date : 2013 Jan 29

PMID : 23286227






3 Functional Relationships(s)
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1 Comparison of the internal cavity in the LBD model of zebrafish (zf) AHR2, which binds TCDD with high affinity, to that of zfAHR1a, which does not bind TCDD, revealed that the latter has a dramatically shortened binding cavity due to the side chains of three residues (Tyr296, Thr386, and His388) that reduce the amount of internal space available to TCDD. Polychlorinated Dibenzodioxins aryl hydrocarbon receptor 2 Danio rerio
2 Mutagenesis of two of these residues in zfAHR1a to those present in zfAHR2 (Y296H and T386A) restored the ability of zfAHR1a to bind TCDD and to exhibit TCDD-dependent binding to DNA. Polychlorinated Dibenzodioxins aryl hydrocarbon receptor 2 Danio rerio
3 Mutagenesis of two of these residues in zfAHR1a to those present in zfAHR2 (Y296H and T386A) restored the ability of zfAHR1a to bind TCDD and to exhibit TCDD-dependent binding to DNA. Polychlorinated Dibenzodioxins aryl hydrocarbon receptor 2 Danio rerio