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X-ray and neutron small-angle scattering analysis of the complex formed by the met receptor and the Listeria monocytogenes invasion protein InlBстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 3 декабря 2017 г.
- Авторы: Niemann Hartmut H., Petoukhov Maxim V., Hartlein Michael, Moulin Martine, Gherardi Ermanno, Timmins Peter, Heinz Dirk W., Svergun Dmitri I.
- Журнал: Journal of Molecular Biology
- Том: 377
- Номер: 2
- Год издания: 2008
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 489
- Последняя страница: 500
- DOI: 10.1016/j.jmb.2008.01.027
- Аннотация: The Listeria monocytogenes surface protein InIB binds to the extracellular domain of the human receptor tyrosine kinase Met, the product of the c-met proto-oncogene. InlB binding activates the Met receptor, leading to uptake of Listeria into normally nonphagocytic host cells. The N-terminal half of InIB (InlB(321)) is sufficient for Met binding and activation. The complex between this Met-binding domain of InIB and various constructs of the Met ectodomain was characterized by size exclusion chromatography and dynamic light scattering, and structural models were built using small-angle X-ray scattering and small-angle neutron scattering. Although most receptor tyrosine kinase ligands induce receptor dimerization, InlB(321) consistently binds the Met ectodomain with a 1:1 stoichiometry. A construct comprising the Sema and PSI domains of Met, although sufficient to bind the physiological Met ligand hepatocyte growth factor/scatter factor, does not form a complex with InlB(321) in solution, highlighting the importance of Met Ig domains for InIB binding. Small-angle X-ray scattering and small-angle neutron scattering measurements of ligand and receptor, both free and in complex, reveal an elongated shape for the receptor. The four Ig domains form a bent, rather than a fully extended, conformation, and InlB(321) binds to Sema and the first Ig domain of Met, in agreement with the recent crystal structure of a smaller Met fragment in complex with InlB(321), These results call into question whether receptor dimerization is the basic underlying event in InlB(321)-mediated Met activation and demonstrate differences in the mechanisms by which the physiological ligand hepatocyte growth factor/scatter factor and InlB(321) bind and activate the Met receptor. (C) 2008 Elsevier Ltd. All rights reserved.
- Добавил в систему: Петухов Максим Владимирович