SYSTEMIC LUPUS ERYTHEMATOSUS: ANALYSIS OF POSSIBLE LOCALIZATION OF ACTIVE SITES IN A PROTEIN SEQUENCE OF MONOCLONAL LIGHT CHAIN (NGTA1-Me-pro) WITH METALLOPROTEASE ACTIVITIES



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Abstract

It was shown previously that monoclonal light chains (MLCh) corresponding to the phagemid library of recombinant light chains of immunoglobulin of peripheral blood lymphocytes of patients with systemic lupus erythematosus (SLE) specifically hydrolyze only the myelin basic protein (MBP). The preparations of one of the light chains (NGTA1-Me-pro) demonstrated two optimal pH values, two optimal concentrations of metal ions and two Km values for MBP. Two protease active centers of NGTA1-Me-pro were metal-dependent. In this paper, the homology of protein sequence NGTA1-Me-pro with those for several classical Zn2+- и Ca2+-dependent ap wtll as serine human proteases was analyzed for the first time. The analysis revealed possible protein sequences NGTA1-Me-pro responsible for the binding of MBP, chelation of metal ions and direct catalysis. The data obtained are generalized by means of hypothetical models of the structure of two active centers of the light chain of antibodies. 

About the authors

A. M. Timofeeva

Institute of Chemical Biology and Fundamental Medicine of the Suberian Branch of the Russian Academy of Sciences

Author for correspondence.
Email: fake@neicon.ru

PhD, Junior researcher, 

Novosibirsk

Russian Federation

G. A. Nevinsky

Institute of Chemical Biology and Fundamental Medicine of the Suberian Branch of the Russian Academy of Sciences

Email: nevinsky@niboch.nsc.ru

doctor of chemistry, professor, chef researcher, 

Novosibirsk

Russian Federation

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