Articles written in Journal of Biosciences
Volume 8 Issue 1-2 August 1985 pp 491-498
The molecular mechanism of drug action has been studied by X-ray diffraction analysis of human carbonic anhydrase I complexed with two different sulphonamides. The acetazolamide and amino benzene sulphonamide are found to bind to the catalytically essential zinc ion thereby inhibiting the function of the enzyme. The inhibitor molecules are stabilized in the active site of the protein by van der Waals interaction with a number of protein side chain groups.
Volume 41 Issue 4 December 2016 pp 589-600 ARTICLE
The hypothetical protein ‘Alr3200’ of Anabaena sp. strain PCC7120 is highly conserved among cyanobacterialspecies. It is a member of the DUF820 (Domain of Unknown Function) protein family, and is predicted to have aDNase domain. Biochemical analysis revealed a Mg(II)-dependent DNase activity for Alr3200 with a specific activityof 8.62×104 Kunitz Units (KU) mg−1 protein. Circular dichroism analysis predicted Alr3200 to have ~40% β-strandsand ~9% α-helical structures. Anabaena PCC7120 inherently expressed Alr3200 at very low levels, and its overexpressionhad no significant effect on growth of Anabaena under control conditions. However, Analr3200+, therecombinant Anabaena strain overexpressing Alr3200, exhibited zero survival upon exposure to 6 kGy of γ-radiation,which is the LD50 for wild type Anabaena PCC7120 as well as the vector control recombinant strain, AnpAM.Comparative analysis of the two recombinant Anabaena strains suggested that it is not the accumulated Alr3200 perse, but its possible interactions with the radiation-induced unidentified DNA repair proteins of Anabaena, whichhampers DNA repair resulting in radiosensitivity.
Volume 45, 2020
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