Mutation of potential phosphorylation sites in the recombinant R domain of the cystic fibrosis transmembrane conductance regulator has significant effects on domain conformation

Biochemical and Biophysical Research Communications

Volumn 206, Issue 1, 1995, Pages 207-214

  Dulhanty, Ann M ^a   Riordan, John R ^b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLUTAMIC ACID; SERINE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

ALGORITHM; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; MUTAGENESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SPECTROSCOPY;

AMINO ACID SEQUENCE; CHLORIDE CHANNELS; CIRCULAR DICHROISM; COMPARATIVE STUDY; CYCLIC AMP-DEPENDENT PROTEIN KINASES; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SERINE; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; THREONINE;

EID: 0028891373     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1006/bbrc.1995.1029     Document Type: Article

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