Deletion of phenylalanine 508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases conformational exchange and inhibits dimerization

Journal of Biological Chemistry

Volumn 290, Issue 38, 2015, Pages 22862-22878

  Chong, P Andrew ^a   Farber, Patrick J ^a   Vernon, Robert M ^a   Hudson, Rhea P ^a   Mittermaier, Anthony K ^c   Forman Kay, Julie D ^a,b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINS; CHEMICAL ANALYSIS; CHEMICAL SHIFT; DIMERIZATION; DIMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDES;

CHEMICAL SHIFT PERTURBATIONS; CONCENTRATION-DEPENDENT; CONFORMATIONAL EXCHANGE; CONFORMATIONAL SAMPLINGS; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATORS; INTRAMOLECULAR INTERACTIONS; NUCLEOTIDE-BINDING DOMAIN; PARAMAGNETIC RELAXATION ENHANCEMENTS;

CONFORMATIONS;

CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; NUCLEOTIDE BINDING DOMAIN 1; NUCLEOTIDE BINDING PROTEIN; PHENYLALANINE; UNCLASSIFIED DRUG; CFTR PROTEIN, HUMAN;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; INHIBITION KINETICS; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; QUALITATIVE ANALYSIS; AMINO ACID SEQUENCE; CHEMISTRY; GENE DELETION; GENETICS; HUMAN; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHENYLALANINE; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION;

EID: 84942863094     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.641134     Document Type: Article

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