Antibody CDR H3 modeling rules: extension for the case of absence of Arg H94 and Asp H101

Koliasnikov, O.V.; Grigorenko, V.G.; Egorov, A.M.; Kiral, M.O.

Информация о цитировании статьи получена из Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 5 июня 2017 г.

Авторы: Koliasnikov O.V., Grigorenko V.G., Egorov A.M., Kiral M.O.
Журнал: Journal of Bioinformatics and Computational Biology
Том: 4
Номер: 2
Год издания: 2006
Издательство: Imperial College Press
Местоположение издательства: United Kingdom
Первая страница: 415
Последняя страница: 424
DOI: 10.1142/S0219720006001874
Аннотация: The third complementary determining region of the immunoglobulin heavy chain (CDR H3) is one of the more difficult structures to model due to genetic reasons. However, the conformation of proximal to beta-framework ("torso") part of the CDR H3 is very predictable. Current "CDR's canonical classes" theory is based on identifying the key positions, H94 and H101. We can determine the CDR H3 "torso" structure if arginine or lysine is present in the H94 position and/or aspartic acid in the H101 position. We target the case characterized by the absence of key residues in both the H94 and H101 positions. There has not been discussion on this case in the literature. 51 CDR H3 structures of this nature are analyzed and we established new sequence-structure rules. These rules contribute to more accurate modeling of the antibody's structure.
Добавил в систему: Колясников Олег Владимирович

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Antibody CDR H3 modeling rules: extension for the case of absence of Arg H94 and Asp H101статья

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