State-dependent Chemical Reactivity of an Engineered Cysteine Reveals Conformational Changes in the Outer Vestibule of the Cystic Fibrosis Transmembrane Conductance Regulator

Cystic fibrosis transmembrane conductance regulator (CFTR) chloride channels are gated by binding and hydrolysis of ATP at the nucleotide-binding domains (NBDs). We used covalent modification of CFTR channels bearing a cysteine engineered at position 334 to investigate changes in pore conformation t...

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Veröffentlicht in:	The Journal of biological chemistry 2005-12, Vol.280 (51), p.41997-42003
Hauptverfasser:	Zhang, Zhi-Ren, Song, Binlin, McCarty, Nael A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - physiology Cysteine - chemistry Cysteine - physiology Cystic Fibrosis Transmembrane Conductance Regulator - chemistry Cystic Fibrosis Transmembrane Conductance Regulator - genetics Cystic Fibrosis Transmembrane Conductance Regulator - physiology Ion Channel Gating Kinetics Mesylates - chemistry Mutagenesis, Site-Directed Protein Conformation Protein Engineering
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