NMR, biophysical, and biochemical studies reveal the minimal calmodulin binding domain of the HIV-1 matrix protein

Journal of Biological Chemistry

Volumn 286, Issue 38, 2011, Pages 33533-33543

  Samal, Alexandra B ^a   Ghanam, Ruba H ^a   Fernandez, Timothy F ^a   Monroe, Eric B ^a   Saad, Jamil S ^a  

^a University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; BIOCHEMICAL STUDIES; BIOPHYSICAL METHODS; CALMODULIN BINDING DOMAIN; CONFORMATIONAL CHANGE; DISSOCIATION CONSTANT; HIGH AFFINITY; HUMAN IMMUNODEFICIENCY VIRUS TYPE-1; INFECTED CELLS; LIMITED PROTEOLYSIS; MATRIX; MATRIX PROTEINS; MOLECULAR MECHANISM; SUBCELLULAR DISTRIBUTION;

CAMS; CELLS; DISEASES; DISSOCIATION; PEPTIDES; VIRUSES;

CALMODULIN;

CALMODULIN; GAG PROTEIN; MATRIX PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HUMAN IMMUNODEFICIENCY VIRUS 1; MOLECULAR MECHANICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PLASMID; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN LOCALIZATION;

AMINO ACID SEQUENCE; ANIMALS; BIOCHEMICAL PHENOMENA; BIOPHYSICAL PHENOMENA; CALMODULIN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GAG GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; HIV ANTIGENS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RATS; THERMODYNAMICS; THERMOLYSIN;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 80053001284     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.273623     Document Type: Article

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