5h4c
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5h4c is ON HOLD Authors: Description: Category: Unreleased Structures) |
|||
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Cbln4== | |
| + | <StructureSection load='5h4c' size='340' side='right'caption='[[5h4c]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5h4c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H4C FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h4c OCA], [https://pdbe.org/5h4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h4c RCSB], [https://www.ebi.ac.uk/pdbsum/5h4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h4c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D4ABJ2_RAT D4ABJ2_RAT] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28877468</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5h4c" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Ding J]] | ||
| + | [[Category: Shen J]] | ||
| + | [[Category: Zhang H]] | ||
| + | [[Category: Zhong C]] | ||
Current revision
Crystal structure of Cbln4
| |||||||||||
