Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions

doi:10.1016/j.celrep.2017.08.031

	Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions
	Zhong, Chen 1; Shen, Jinlong 1; Zhang, Huibing 1; Li, Guangyi 1; Shen, Senlin 2; Wang, Fang 1; Hu, Kuan 1,6; Cao, Longxing 1; He, Yongning 1; Ding, Jianping1,3,4,5
	2017-09-05
发表期刊	CELL REPORTS (IF:7.5[JCR-2023],8.5[5-Year])
ISSN	2211-1247
卷号	20 期号:10 页码:2328-2340
发表状态	已发表
DOI	10.1016/j.celrep.2017.08.031
摘要	Unlike cerebellin 1 (Cbln1), which bridges neurexin (Nrxn) receptors and delta-type glutamate receptors in a trans-synaptic triad, Cbln4 was reported to have no or weak binding for the receptors despite sharing similar to 70% sequence identity with Cbln1. Here, we report crystal structures of the homotrimers of the C1q domain of Cbln1 and Cbln4 at 2.2 and 2.3 angstrom resolution, respectively. Comparison of the structures suggests that the difference between Cbln1 and Cbln4 in GluD2 binding might be because of their sequence and structural divergence in loop CD. Surprisingly, we show that Cbln4 binds to Nrxn1 beta and forms a stable complex with the laminin, nectin, sex-hormone binding globulin (LNS) domain of Nrxn1 beta. Furthermore, the negative-stain electron microscopy reconstruction of hexameric full-length Cbln1 at 13 angstrom resolution and that of the Cbln4/Nrxn1 beta complex at 19 angstrom resolution suggest that Nrxn1 beta binds to the N-terminal region of Cbln4, probably through strand beta 10 of the S4 insert.
收录类别	SCI
语种	英语
资助项目	Chinese Academy of Sciences[2011201] ; Chinese Academy of Sciences[XDB08010302]
WOS研究方向	Cell Biology
WOS类目	Cell Biology
WOS记录号	WOS:000409248000006
出版者	CELL PRESS
WOS关键词	CELL SYNAPSE FORMATION ; CRYSTAL-STRUCTURE ; MACULAR DEGENERATION ; SIGNALING PATHWAYS ; FAMILY ; GLUR-DELTA-2 ; CEREBELLUM ; PROTEINS ; NEUREXIN ; GENE
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/4638
专题	生命科学与技术学院_特聘教授组_丁建平组
通讯作者	Zhong, Chen; Ding, Jianping
作者单位	1.Univ Chinese Acad Sci, Chinese Acad Sci, Ctr Excellence Mol Cell Sci,State Key Lab Mol Bio, Inst Biochem & Cell Biol,Natl Ctr Prot Sci Shangh, 320 Yueyang Rd, Shanghai 200031, Peoples R China 2.Shanghai Univ, Sch Life Sci, 333 Nanchen Rd, Shanghai 200444, Peoples R China 3.ShanghaiTech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China 4.Chinese Acad Sci, Shanghai Sci Res Ctr, Shanghai 201204, Peoples R China 5.Fudan Univ, Collaborat Innovat Ctr Genet & Dev, 2005 Song Hu Rd, Shanghai 200438, Peoples R China 6.SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Zhong, Chen,Shen, Jinlong,Zhang, Huibing,et al. Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions[J]. CELL REPORTS,2017,20(10):2328-2340.
APA	Zhong, Chen.,Shen, Jinlong.,Zhang, Huibing.,Li, Guangyi.,Shen, Senlin.,...&Ding, Jianping.(2017).Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions.CELL REPORTS,20(10),2328-2340.
MLA	Zhong, Chen,et al."Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions".CELL REPORTS 20.10(2017):2328-2340.