Title : Trafficking defects in PAS domain mutant Kv11.1 channels: roles of reduced domain stability and altered domain-domain interactions.

Pub. Date : 2013 Aug 15

PMID : 23721480






3 Functional Relationships(s)
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1 Six mutants, located in the vicinity of a hydrophobic patch on the PAS domain surface, also affected binding of the isolated PAS domain to an N-terminal truncated hERG (human ether-a-go-go-related gene) channel. Aminosalicylic Acid ETS transcription factor ERG Homo sapiens
2 Six mutants, located in the vicinity of a hydrophobic patch on the PAS domain surface, also affected binding of the isolated PAS domain to an N-terminal truncated hERG (human ether-a-go-go-related gene) channel. Aminosalicylic Acid ETS transcription factor ERG Homo sapiens
3 Our results highlight a critical role for interactions between the PAS domain and the remainder of the channel in the hERG assembly and that mutants that affect PAS domain interactions with the remainder of the channel have a more severe trafficking defect than that caused by domain unfolding alone. Aminosalicylic Acid ETS transcription factor ERG Homo sapiens