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Vol 49(2015) N 5 p. 736-741; DOI 10.1134/S0026893315050027  G.G. Arakelov1,2, O.V. Osipov2, K.B. Nazaryan1,2* Effects of M680I and M694V pyrin mutations on the tertiary structure of domain B30.2 and its interaction with caspase-1: In silico analysis 1Russian-Armenian (Slavonic) University, Yerevan, 0051, Armenia2Institute of Molecular Biology, National Academy of Sciences of the Republic of Armenia, Yerevan, 0014, Armenia *karen.nazaryan@gmail.com Received - 2014-12-11; Accepted - 2015-04-28 The M680I and M694V mutations located in the B30.2 pyrin domain are responsible for the manifestation of the most common forms of Familial Mediterranean fever. It is well known that a malfunction of the pyrin-caspase-1 complex is the main cause of inflammation in FMF. The purpose of this study was to identify possible changes in the tertiary structure of mutated B30.2 domain and to determine their potential consequences in the formation of the pyrin-caspase-1 complex. Using computer modeling, it was found that the above mutations change the tertiary structure of B30.2 domain, causing shifts of binding sites and altering the energy of interaction between B30.2 and caspase-1. FMF, pyrin, B30.2, caspase-1, in silico, molecular modeling, protein-protein interaction |
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