5H4B

Crystal structure of Cbln4

Summary for 5H4B

• Entry DOI: 10.2210/pdb5h4b/pdb
• Related: 5H48 5H49 5H4C
• Descriptor: Cerebellin-4, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: cbln1, cbln4, c1q domain, c1q/tnf superfamily, neurexin, receptor specificity, synaptogenesis, protein binding
• Biological source: Mus musculus (Mouse)
• Cellular location: Secreted: Q8BME9
• Total number of polymer chains: 1
• Total formula weight: 20839.55

Authors

Zhong, C.,Shen, J.,Zhang, H.,Ding, J. (deposition date: 2016-10-31, release date: 2017-09-13, Last modification date: 2024-10-09)

Primary citation

Zhong, C.,Shen, J.,Zhang, H.,Li, G.,Shen, S.,Wang, F.,Hu, K.,Cao, L.,He, Y.,Ding, J.
Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions.
Cell Rep, 20:2328-2340, 2017

PubMed Abstract: Unlike cerebellin 1 (Cbln1), which bridges neurexin (Nrxn) receptors and δ-type glutamate receptors in a trans-synaptic triad, Cbln4 was reported to have no or weak binding for the receptors despite sharing ∼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 Å 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 Nrxn1β and forms a stable complex with the laminin, nectin, sex-hormone binding globulin (LNS) domain of Nrxn1β. Furthermore, the negative-stain electron microscopy reconstruction of hexameric full-length Cbln1 at 13 Å resolution and that of the Cbln4/Nrxn1β complex at 19 Å resolution suggest that Nrxn1β binds to the N-terminal region of Cbln4, probably through strand β10 of the S4 insert.

PubMed: 28877468
DOI: 10.1016/j.celrep.2017.08.031

Experimental method

X-RAY DIFFRACTION (2.8 Å)