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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-03

AUTHORS

N C Strynadka, M Eisenstein, E Katchalski-Katzir, B K Shoichet, I D Kuntz, R Abagyan, M Totrov, J Janin, J Cherfils, F Zimmerman, A Olson, B Duncan, M Rao, R Jackson, M Sternberg, M N James

ABSTRACT

Crystallization of the 1:1 molecular complex between the beta-lactamase TEM-1 and the beta-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 groups were given the refined atomic coordinates of each of the native molecules. Other than the fact that BLIP is an effective inhibitor of a number of beta-lactamase enzymes (KI for TEM-1 approximately 100 pM) no other biochemical or structural data were available to assist the practitioners in their molecular docking. In addition, it was not known whether the molecules underwent conformational changes upon association or whether the inhibition was competitive or non-competitive. All six of the groups that accepted the challenge correctly predicted the general mode of association of BLIP and TEM-1. More... »

PAGES

233-239

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb0396-233

DOI

http://dx.doi.org/10.1038/nsb0396-233

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1049825643

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8605624


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