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5h49

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Revision as of 10:16, 8 November 2017

Crystal structure of Cbln1

Structural highlights

5h49 is a 3 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5h48, 5h4b, 5h4c
Gene:	Cbln1 (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CBLN1_RAT] Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). The cerebellin exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release. A conversion to [des-Ser1]-cerebellin by endopeptidases seems to be required for its autocrine-paracrine regulatory functions.^[1] ^[2]

Publication Abstract from PubMed

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 approximately 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 A 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 Nrxn1beta and forms a stable complex with the laminin, nectin, sex-hormone binding globulin (LNS) domain of Nrxn1beta. Furthermore, the negative-stain electron microscopy reconstruction of hexameric full-length Cbln1 at 13 A resolution and that of the Cbln4/Nrxn1beta complex at 19 A resolution suggest that Nrxn1beta binds to the N-terminal region of Cbln4, probably through strand beta10 of the S4 insert.

Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions.,Zhong C, Shen J, Zhang H, Li G, Shen S, Wang F, Hu K, Cao L, He Y, Ding J Cell Rep. 2017 Sep 5;20(10):2328-2340. doi: 10.1016/j.celrep.2017.08.031. PMID:28877468^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Albertin G, Malendowicz LK, Macchi C, Markowska A, Nussdorfer GG. Cerebellin stimulates the secretory activity of the rat adrenal gland: in vitro and in vivo studies. Neuropeptides. 2000 Feb;34(1):7-11. PMID:10688962 doi:http://dx.doi.org/10.1054/npep.1999.0779
↑ Rucinski M, Albertin G, Spinazzi R, Ziolkowska A, Nussdorfer GG, Malendowicz LK. Cerebellin in the rat adrenal gland: gene expression and effects of CER and [des-Ser1]CER on the secretion and growth of cultured adrenocortical cells. Int J Mol Med. 2005 Mar;15(3):411-5. PMID:15702230
↑ 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. 2017 Sep 5;20(10):2328-2340. doi: 10.1016/j.celrep.2017.08.031. PMID:28877468 doi:http://dx.doi.org/10.1016/j.celrep.2017.08.031

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5h49"

@@ Line 3: / Line 3: @@
 <StructureSection load='5h49' size='340' side='right' caption='[[5h49]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5h49]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H49 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5h49]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H49 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h48|5h48]], [[5h4b|5h4b]], [[5h4c|5h4c]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cbln1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5h49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h49 OCA], [http://pdbe.org/5h49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h49 RCSB], [http://www.ebi.ac.uk/pdbsum/5h49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h49 ProSAT]</span></td></tr>
 </table>
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Buffalo rat]]
 [[Category: Ding, J]]
 [[Category: Shen, J]]

5h49

From Proteopedia

Revision as of 10:16, 8 November 2017

Crystal structure of Cbln1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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