MARCKS is a natively unfolded protein with an inaccessible actin-binding site: Evidence for long-range intramolecular interactions

Journal of Biological Chemistry

Volumn 280, Issue 11, 2005, Pages 9946-9956

  Tapp, Hazel ^a,b   Al Naggar, Iman M ^a,b   Yarmola, Elena G ^a,b   Harrison, Alexis ^a,b   Shaw, Gerry ^a   Edison, Arthur S ^a   Bubb, Michael R ^a,b  

^a UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

^b VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOCHEMISTRY; CHEMICAL MODIFICATION; IONIC CONDUCTION; MOLECULAR STRUCTURE; PHOSPHORUS;

INTRAMOLECULAR INTERACTIONS; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATES (MARCKS); PHOSPHORYLATION SITE DOMAIN (PSD); POST-TRANSLATIONAL MODIFICATION;

PROTEINS;

ACTIN; CALMODULIN; CALPAIN; MARCKS PROTEIN;

ACTIN FILAMENT; ACTIN POLYMERIZATION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING SITE; CHEMICAL BOND; CONTROLLED STUDY; ISOELECTRIC POINT; MYRISTYLATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION;

ACTINS; ANIMALS; ANISOTROPY; BINDING SITES; CALMODULIN; CALPAIN; DNA; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; IONS; MEMBRANE PROTEINS; MICE; MUSCLE, SKELETAL; MYRISTIC ACIDS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RABBITS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; TIME FACTORS;

ANIMALIA;

EID: 15444365811     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M414614200     Document Type: Article

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