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A novel ArgH52/TyrH33 conservative motif in antibodies: a correlation between sequence of antibodies and antigen bindingстатья
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: 11 ноября 2020 г.
- Авторы: Petrov A., Arzhanik V., Makarov G., Koliasnikov O.
- Журнал: Journal of Bioinformatics and Computational Biology
- Том: 14
- Номер: 4
- Год издания: 2016
- Издательство: Imperial College Press
- Местоположение издательства: United Kingdom
- Первая страница: 1650019
- DOI: 10.1142/S0219720016500190
- Аннотация: Antibodies are the family of proteins, which are responsible for antigen recognition. The computational modeling of interaction between an antigen and an antibody is very important when crystallographic structure is unavailable. In this research we have discovered the correlation between the amino acid sequence of antibody and its specific binding characteristics on the example of the novel conservative binding motif, which consists of four residues: Arg H52, Tyr H33, Thr H59 and Glu H61. These residues are specifically oriented in the binding site and interact with each other in a specific manner. The residues of the binding motif are involved in interaction strictly with negatively charged groups of antigens, and form a binding complex. Mechanism of interaction and characteristics of the complex were also discovered. The results of this research can be used to increase the accuracy of computational antibody-antigen interaction modeling and for post-modeling quality control of the modeled structures.
- Добавил в систему: Колясников Олег Владимирович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Первая страница | petrov2016_1st_page.pdf | 48,1 КБ | 25 августа 2016 [olkol] |