Molecular docking programs successfully predict the binding of a β-lactamase inhibitory protein to TEM-1 β-lactamase

Crystallization of the 1:1 molecular complex between the β-lactamase TEM-1 and the β-lactamase inhibitory protein BLIP has provided an opportunity to put a stringent test on current protein-docking algorithms. Prior to the successful determination of the structure of the complex, nine laboratory gro...

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Veröffentlicht in:	Nature Structural Biology 1996-03, Vol.3 (3), p.233-239
Hauptverfasser:	Strynadka, N.C.J., Eisenstein, M., Katchalski-Katzir, E., Shoichet, B.K., Kuntz, I.D., Abagyan, R., Totrov, M., Janin, J., Cherfils, J., Zimmerman, F., Olson, A., Duncan, B., Rao, M., Jackson, R., Sternberg, M., James, M.N.G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism beta-Lactamases - chemistry beta-Lactamases - metabolism Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Crystallization Crystallography, X-Ray Glutamine Hydrogen Bonding insight Life Sciences Membrane Biology Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure Reproducibility of Results
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