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TitleCbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions.
Journal, issue, pagesCell Rep, Vol. 20, Issue 10, Page 2328-2340, Year 2017
Publish dateSep 5, 2017
AuthorsChen Zhong / Jinlong Shen / Huibing Zhang / Guangyi Li / Senlin Shen / Fang Wang / Kuan Hu / Longxing Cao / Yongning He / Jianping Ding /
PubMed AbstractUnlike 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 ...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.
External linksCell Rep / PubMed:28877468
MethodsEM (single particle) / X-ray diffraction
Resolution2.2 - 20.0 Å
Structure data

EMDB-6665:
The hexamer of full-length Cbln1
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-6666:
The hexamer of full-length Cbln4 in complex with the LNS domain of Nrxn1beta
Method: EM (single particle) / Resolution: 20.0 Å

PDB-5h48:
Crystal structure of Cbln1
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-5h49:
Crystal structure of Cbln1
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5h4b:
Crystal structure of Cbln4
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5h4c:
Crystal structure of Cbln4
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • rattus norvegicus (Norway rat)
  • mus musculus (house mouse)
KeywordsPROTEIN BINDING / C1q domain / C1q/TNF superfamily / receptor specificity / synaptogenesis / Cbln1 / Cbln4 / neurexin

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