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干扰素-γ与其可溶性高亲和力受体复合物的晶体结构

Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor.

作者信息

Walter M R, Windsor W T, Nagabhushan T L, Lundell D J, Lunn C A, Zauodny P J, Narula S K

机构信息

Department of Pharmacology, University of Alabama at Birmingham 35294, USA.

出版信息

Nature. 1995 Jul 20;376(6537):230-5. doi: 10.1038/376230a0.

DOI:10.1038/376230a0
PMID:7617032
Abstract

The crystal structure of interferon-gamma bound to the extracellular fragment of its high-affinity cell-surface receptor reveals the first view of a class-2 cytokine receptor-ligand complex. In the complex, one interferon-gamma homodimer binds two receptor molecules. Unlike the class-1 growth hormone receptor complex, the two interferon-gamma receptors do not interact with one another and are separated by 27 A. Upon receptor binding, the flexible AB loop of interferon-gamma undergoes a conformational change that includes the formation of a 3(10) helix.

摘要

与高亲和力细胞表面受体细胞外片段结合的干扰素-γ晶体结构揭示了2类细胞因子受体-配体复合物的首个视图。在该复合物中,一个干扰素-γ同二聚体结合两个受体分子。与1类生长激素受体复合物不同,两个干扰素-γ受体不相互作用,且相隔27埃。受体结合后,干扰素-γ的柔性AB环发生构象变化,包括形成一个3(10)螺旋。

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