Title : Sensitivity of KATP channels to cellular metabolic disorders and the underlying structural basis.

Pub. Date : 2016 Jan

PMID : 26725741






1 Functional Relationships(s)
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1 Moreover, the residues (K707 and K1348) within the Walker A (WA) motifs of two nucleotide-binding domains (NBDs) were essential for SUR2B/Kir6.x (especially SUR2B/Kir6.1) channel activation by Na-azide, suggesting a key role for Mg-adenine nucleotide binding and/or hydrolysis in the SUR2B subunit. mg-adenine nucleotide potassium inwardly rectifying channel subfamily J member 8 L homeolog Xenopus laevis