Literature summary for 5.6.1.6 extracted from

Bompadre, S.G.; Li, M.; Hwang, T.C.
Mechanism of G551D-CFTR (cystic fibrosis transmembrane conductance regulator) potentiation by a high affinity ATP analog (2008), J. Biol. Chem., 283, 5364-5369.

Search for more literature for 5.6.1.6

Cloned(Commentary)

Cloned (Comment)	Organism
expression in CHO cell	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
G551D	mutation in ATP-binding pocket 2, abolishes ATP-dependent gating, results in an open probability of the channel that is 100fold lower than that of wild-type. The ATP analog N6-(2-phenylethyl)-ATP increases G551D currents mainly by increasing the open time of the channel. This effect is reduced when N6-(2-phenylethyl)-ATP is applied together with ATP	Homo sapiens
G551D/Y1219G	lowered binding affinity at the ATP binding-pocket 2, no influence on the increasing of the open time of the channel by N6-(2-phenylethyl)-ATP	Homo sapiens
W401G/G551D	significant reduction of the increasing of the open time of the channel by N6-(2-phenylethyl)-ATP	Homo sapiens
Y1219G	decreases the apparent affinity of ATP and P-ATP	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
N6-(2-phenylethyl)-ATP	competitive with ATP, binds to ATP-binding pocket 1	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P13569	isoform CFTR	-

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Release 2023.1 (January 2023)