Title : Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR.

Pub. Date : 2011 May

PMID : 21245039






4 Functional Relationships(s)
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1 Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR. Protactinium aryl hydrocarbon receptor Homo sapiens
2 Using a new bacterial two-hybrid system that selects for loss of protein interactions, we have identified 22 amino acids in the N-terminal PAS domain of Arnt that are involved in heterodimerization with aryl hydrocarbon receptor (AhR). Protactinium aryl hydrocarbon receptor Homo sapiens
3 Using a new bacterial two-hybrid system that selects for loss of protein interactions, we have identified 22 amino acids in the N-terminal PAS domain of Arnt that are involved in heterodimerization with aryl hydrocarbon receptor (AhR). Protactinium aryl hydrocarbon receptor Homo sapiens
4 Arnt uses the same face of the N-terminal PAS domain for homo- and heterodimerization and mutational analysis of AhR demonstrated that the equivalent region is used by AhR when dimerizing with Arnt. Protactinium aryl hydrocarbon receptor Homo sapiens