Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant

• Published in: Protein engineering, design and selection Vol. 23; no. 5; pp. 375 - 384
• Main Authors: Atwell, Shane, Brouillette, Christie G., Conners, Kris, Emtage, Spencer, Gheyi, Tarun, Guggino, William B., Hendle, Jorg, Hunt, John F., Lewis, Hal A., Lu, Frances, Protasevich, Irina I., Rodgers, Logan A., Romero, Rich, Wasserman, Stephen R., Weber, Patricia C., Wetmore, Diana, Zhang, Feiyu F., Zhao, Xun
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.05.2010
• Subjects: ABC transporter; BASIC BIOLOGICAL SCIENCES; Binding Sites - genetics; CFTR; Cloning, Molecular; Crystallization; Cystic Fibrosis Transmembrane Conductance Regulator - chemistry; Cystic Fibrosis Transmembrane Conductance Regulator - isolation & purification; Dimerization; DNA Primers - genetics; FIBROSIS; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; Humans; Models, Molecular; MUTANTS; Mutation - genetics; MUTATIONS; NBD1; NUCLEOTIDES; Protein Conformation; Protein Structure, Tertiary - genetics; PROTEINS; regulatory insert; REMOVAL; RESIDUES; RESOLUTION; ΔF508; regulatory insert; NBD1; ABC transporter; CFTR; ΔF508

Upon removal of the regulatory insert (RI), the first nucleotide binding domain (NBD1) of human cystic fibrosis transmembrane conductance regulator (CFTR) can be heterologously expressed and purified in a form that remains stable without solubilizing mutations, stabilizing agents or the regulatory e...