A potent new mode of β-lactamase inhibition revealed by the 1.7 Å X-ray crystallographic structure of the TEM-1-BLIP complex

Nature Structural Biology

Volumn 3, Issue 3, 1996, Pages 290-297

  Strynadka, Natalie C J ^a   Jensen, Susan E ^a   Alzari, Pedro M ^b   James, Michael N G ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

^b INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; BETA LACTAMASE INHIBITORY PROTEIN; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DRUG DESIGN; DRUG PROTEIN BINDING; ENZYME INHIBITION; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIA; BACTERIAL PROTEINS; BETA-LACTAMASES; BINDING SITES; CLONING, MOLECULAR; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0029949210     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0396-290     Document Type: Article

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