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Amphipathic secondary structure elements and putative cholesterol recognizing amino acid consensus (CRAC) motifs as governing factors of highly specific matrix protein interactions with raft-type membranes in enveloped virusesстатья
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: 7 сентября 2017 г.
- Авторы: Radyukhin VA, Dadinova LA, Orlov IA, Baratova LA
- Журнал: Journal of Biomolecular Structure and Dynamics
- Том: 36
- Номер: 5
- Год издания: 2018
- Издательство: Adenine Press
- Местоположение издательства: United States
- Первая страница: 1351
- Последняя страница: 1359
- DOI: 10.1080/07391102.2017.1323012
- Аннотация: We have previously revealed amphipathicity of six alpha-helices of influenza virus (IFV) M1 protein, containing cholesterol recognising amino acid consensus (CRAC) motifs, and suggested that the amphipathicity may play a role in supporting both raft structure of the membrane and organising regular structure the M1 protein shell in the virion. Computer modelling and comparative analysing 3D structures of the matrix proteins for three taxonomically different enveloped viruses with raft-type membranes, IFV, Newcastle disease virus (NDV), and Human immunodeficiency virus (HIV), was carried out to disclose amphipathic CRAC containing 3D configurations in their structures, and to identify putative motifs, which may be specifically involved in their interactions with raft membranes. Common features of all three proteins were found to be the amphipathic structures containing CRAC motifs, and outer localization of the comb-like CRAC structures of IFV and NDV M proteins just on the opposite sides of their globules. Previous reconstructions and our modelling reveal that IFV M1 protein exists as a monomer with a compact NM-fragment and an extended partially flexible C-terminal domain, and NDV M protein dimerizes with anti-parallel location of the CRAC motifs on the opposite sides of the dimer. We suppose that such localization of the CRAC motifs conditions interaction of the M proteins both with the raft membrane and with the internal components of the virus, and is consistent with our hypothesis that oppositely situated CRAC motifs in pairs might serve as anchors between two neighbouring raft platforms consolidating all the viral envelopes.
- Добавил в систему: Радюхин Виктор Алексеевич