David M Karlinsky

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Classical complement pathway is an important innate immune mechanism, which is usually triggered by binding of C1q to immunoglobulins, pentraxins and other target molecules. Although the activation of the classical pathway is crucial in the host defence, its undesirable and uncontrolled activation can lead to tissue damage. Thus, understanding the molecular(More)
Oligopeptidase B (OpdB; EC 3.4.21.83) is a trypsin-like peptidase belonging to the family of serine prolyl oligopeptidases; two-domain structure of the enzyme includes C-terminal peptidase catalytic domain and N-terminal seven-bladed β-propeller domain. Importance of the interface between these domains and particularly of the 5 salt bridges for enzyme(More)
Current computational methods have not been able to discover an unknown site for low-molecular-weight ligands on a protein receptor and predict parameters of their interaction when the binding site is not distinguished by energy of binding or structural features. The authors propose a method to find an unknown, structurally undefined site for binding(More)
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