Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs

doi:10.1016/j.jbc.2021.100776

	Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs
	Niu, Minghui 1,2; Xu, Shengzhao 1,2; Yang, Jie3 ; Yao, Deqiang3 ; Li, Na 4; Yan, Jie 5; Zhong, Guisheng3 ; Song, Gaojie 1,2
	2021-01
发表期刊	JOURNAL OF BIOLOGICAL CHEMISTRY (IF:4.0[JCR-2023],4.4[5-Year])
EISSN	1083-351X
卷号	296
DOI	10.1016/j.jbc.2021.100776
摘要	The adhesion G protein-coupled receptor CD97 and its ligand complement decay-accelerating factor CD55 are important binding partners in the human immune system. Dysfunction in this binding has been linked to immune disorders such as multiple sclerosis and rheumatoid arthritis, as well as various cancers. Previous literatures have indicated that the CD97 includes 3 to 5 epidermal growth factor (EGF) domains at its N terminus and these EGF domains can bind to the N-terminal short consensus repeat (SCR) domains of CD55. However, the details of this interaction remain elusive, especially why the CD55 binds with the highest affinity to the shortest isoform of CD97 (EGF(1,2,5)). Herein, we designed a chimeric expression construct with the EGF(1,2,5) domains of CD97 and the SCR1-4 domains of CD55 connected by a flexible linker and determined the complex structure by crystallography. Our data reveal that the two proteins adopt an overall antiparallel binding mode involving the SCR1-3 domains of CD55 and all three EGF domains of CD97. Mutagenesis data confirmed the importance of EGF(5) in the interaction and explained the binding specificity between CD55 and CD97. The architecture of CD55-CD97 binding mode together with kinetics suggests a force-resisting shearing stretch geometry when forces applied to the C termini of both proteins in the circulating environment. The potential of the CD55-CD97 complex to withstand tensile force may provide a basis for the mechanosensing mechanism for activation of adhesion G protein-coupled receptors.
收录类别	SCIE ; EI
语种	英语
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000672866400742
出版者	ELSEVIER
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/128058
专题	生命科学与技术学院_博士生 iHuman研究所_PI研究组_钟桂生组 iHuman研究所_科学装置(X)_膜蛋白同步辐射线站
通讯作者	Song, Gaojie
作者单位	1.East China Normal Univ, Inst Biomed Sci, Shanghai Key Lab Regulatory Biol, Shanghai, Peoples R China; 2.East China Normal Univ, Sch Life Sci, Shanghai, Peoples R China; 3.ShanghaiTech Univ, iHuman Inst, Shanghai, Peoples R China; 4.Chinese Acad Sci, Zhangjiang Lab, Shanghai Adv Res Inst, Natl Facil Prot Sci Shanghai, Shanghai, Peoples R China; 5.Natl Univ Singapore, Dept Phys, Singapore, Singapore
推荐引用方式 GB/T 7714	Niu, Minghui,Xu, Shengzhao,Yang, Jie,et al. Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2021,296.
APA	Niu, Minghui.,Xu, Shengzhao.,Yang, Jie.,Yao, Deqiang.,Li, Na.,...&Song, Gaojie.(2021).Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs.JOURNAL OF BIOLOGICAL CHEMISTRY,296.
MLA	Niu, Minghui,et al."Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs".JOURNAL OF BIOLOGICAL CHEMISTRY 296(2021).