Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid

Journal of Biological Chemistry

Volumn 283, Issue 24, 2008, Pages 16274-16278

  Bhattacharya, Shibani ^a   Zhang, Hongtao ^b   Debnath, Asim K ^b   Cowburn, David ^a  

^a NEW YORK STRUCTURAL BIOLOGY CENTER   (United States)

^b NEW YORK BLOOD CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BINDING ENERGY; CYTOLOGY; FLOW INTERACTIONS; HYDROCARBONS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC COMPOUNDS; PORT TERMINALS; STRUCTURAL ANALYSIS; VIRUSES;

BINDING AFFINITIES; BIOCHEMICAL DATUMS; BURIED INTERFACES; CAPSID PROTEINS; CORE PARTICLES; HELICAL PEPTIDES; HIGH AFFINITIES; HIGH RESOLUTION STRUCTURES; HUMAN IMMUNODEFICIENCY VIRUSES; IMMATURE VIRUS PARTICLES; IN CELLS; IN VITRO SYSTEMS; INTERMOLECULAR INTERACTIONS; MONOMERIC FORMS; PARTICLE ASSEMBLIES; PEPTIDE INHIBITORS; PLASMA MEMBRANES; SELECTIVE INHIBITORS; SIDE CHAINS; SOLUBLE PEPTIDES; SOLUTION NMR; SOLUTION STRUCTURES; STRUCTURAL CHARACTERIZATIONS; TERMINAL DOMAINS;

CELL MEMBRANES;

HYDROCARBON; PEPTIDE DERIVATIVE; PROTEIN INHIBITOR; GAG PROTEIN; PEPTIDE;

ANIMAL CELL; ARTICLE; CELL STRUCTURE; CONTROLLED STUDY; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; VIRUS CAPSID; CD4+ T LYMPHOCYTE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; KINETICS; METABOLISM; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE;

HUMAN IMMUNODEFICIENCY VIRUS 1; MIRIDAE;

AMINO ACID MOTIFS; CAPSID; CD4-POSITIVE T-LYMPHOCYTES; GENE PRODUCTS, GAG; HIV CORE PROTEIN P24; HIV-1; HYDROCARBONS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

EID: 47749125805     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C800048200     Document Type: Article

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