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OJBTM
Online Journal of
Bioinformatics©
Volume 22 (3): 153-168, 2021.
Homology docking SHV β-lactamases for drug resistance.
Mohd
Hassan Baig, Shazi Shakil and Asad U Khan.
Interdisciplinary Biotechnology Unit,
Aligarh Muslim University, Aligarh, India
ABSTRACT
Baig MH, Shakil S, Khan AU., Homology docking SHV β-lactamases
for drug resistance, Onl J Bioinform.,
22 (3): 153-168,
2021. Extended-spectrum-β-lactamases (ESBLs) in
bacteria impart resistance to cephalosporins. SHV enzymes in ESBLs and binding of SHV-48, SHV-61, SHV-89, SHV-95
or SHV-105 to β-lactamase inhibitors has not been reported. We
generated homology 3D model structure of SHV enzymes validated for stereo
chemical properties. We targeted active
site amino acid residues of SHV enzyme model to predict binding of inhibitors by
energy docking. All SHV variants except SHV-61 interacted with
clavulanic acid through S70, S130, K234 and A237, as residues. Of 20 docking
interactions S70 and A237 were crucial for correct positioning of inhibitors on
binding sites in 12 and 14 instances, respectively. By energy and Ki
calculations, Penem1 was most efficient inhibitor against all bacterial
enzymes, excluding SHV-105, where LN1-255 was most efficient.
Key Words: SHV β-lactamases, Homology, Docking,
3D model, Drug resistance.
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