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Structural elements required for receptor recognition of human interferon-gamma.

作者信息

Lundell D L, Narula S K

机构信息

Schering-Plough Research Institute, Kenilworth, NJ 07033.

出版信息

Pharmacol Ther. 1994 Oct;64(1):1-21. doi: 10.1016/0163-7258(94)90031-0.

DOI:10.1016/0163-7258(94)90031-0
PMID:7531344
Abstract

Interferon (IFN)-gamma is a central factor in numerous immune responses. Recently the three-dimensional structure of human and rabbit IFN-gamma has been elucidated. This review attempts to bring together the structure and function information into a working model of IFN-gamma: receptor interaction. Based on mutagenesis studies, and corroborated by work with peptides, antibodies and proteolytic digestion, three regions have been found to be important for receptor binding: a long loop connecting the A and B helices, His111 in the F helix and a conserved section of the flexible carboxyl terminus. These three regions may form one continuous binding domain.

摘要

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