a dimer of the toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteinstoll样受体4的二聚体胞质域提供了一个特定的脚手架招聘的信号适配器蛋白质.pdfVIP

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2017-09-07 发布于上海
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a dimer of the toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteinstoll样受体4的二聚体胞质域提供了一个特定的脚手架招聘的信号适配器蛋白质.pdf

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a dimer of the toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteinstoll样受体4的二聚体胞质域提供了一个特定的脚手架招聘的信号适配器蛋白质

A Dimer of the Toll-Like Receptor 4 Cytoplasmic Domain Provides a Specific Scaffold for the Recruitment of Signalling Adaptor Proteins ´ ˜ 1. 1. 1¤ 2 3 1 2 Ricardo Nunez Miguel , Joyce Wong , Julian F. Westoll , Heather J. Brooks , Luke A. J. O’Neill , Nicholas J. Gay *, Clare E. Bryant *, Tom P. Monie1* 1 Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom, 2 Department of Veterinary Medicine, University of Cambridge, Cambridge, United Kingdom, 3 School of Biochemistry and Immunology, Trinity College, Dublin, Ireland The Toll-like receptor 4 (TLR4) is a class I transmembrane receptor expressed on the surface of immune system cells. TLR4 is activated by exposure to lipopolysaccharides derived from the outer membrane of Gram negative bacteria and forms part of the innate immune response in mammals. Like other class 1 receptors, TLR4 is activated by ligand induced dimerization, and recent studies suggest that this causes concerted conformational changes in the receptor leading to self association of the cytoplasmic Toll/Interleukin 1 receptor (TIR) signalling domain. This homodimerization event is proposed to provide a new scaffold that is able to bind downstream signalling adaptor proteins. TLR4 uses two different sets of adaptors; TRAM and TRIF, and Mal and MyD88. These adaptor pairs couple two distinct signalling pathways leading to the activation of interferon response factor 3 (IRF-3) and nuclear factor kB (NFkB) respectively. In this paper we have generated a structural model of the TLR4 TIR dimer and used molecular docking to probe for potential sites of interaction between the receptor homodimer and the adaptor molecules. Rema