BLIP-II Employs Differential Hotspot Residues To Bind Structurally Similar Staphylococcus aureus PBP2a and Class A β-Lactamases
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, ‡Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030, United States
Funder
National Institute of Allergy and Infectious Diseases
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00978
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3. Gene Mutations in Human Hæmoglobin: the Chemical Difference Between Normal and Sickle Cell Hæmoglobin
4. Determinants of Binding Affinity and Specificity for the Interaction of TEM-1 and SME-1 β-Lactamase with β-Lactamase Inhibitory Protein
5. Dissecting the Protein-Protein Interface between β-Lactamase Inhibitory Protein and Class A β-Lactamases
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