Conformational changes in the receptor tyrosine kinase IRR during activation were determined
Researchers of the Laboratory of Receptor Cell Biology IBCh RAS together with colleagues from the IPCE RAS and IC RAS carried out a study of the IRR structure by atomic force microscopy and small-angle X-ray scattering. The conformations of the receptor in the active and inactive states have been determined; on the basis of the obtained data, an activation mechanism has been proposed. This work was supported by projects of the Russian Foundation for Basic Research 20-04-00959, 17-00-00486, the Ministry of Science and Higher Education of the Russian Federation and published in two articles in the Journal of Biological Chemistry [1] [2]. Learn more
april 6, 2021