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==Crystal structure of the Protocadherin GammaB4 extracellular domain== | |||
<StructureSection load='6e6b' size='340' side='right'caption='[[6e6b]], [[Resolution|resolution]] 4.52Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6e6b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E6B 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]] 4.52Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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=6e6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6b OCA], [https://pdbe.org/6e6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e6b RCSB], [https://www.ebi.ac.uk/pdbsum/6e6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q91XX6_MOUSE Q91XX6_MOUSE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Neurite self-recognition and avoidance are fundamental properties of all nervous systems(1). These processes facilitate dendritic arborization(2,3), prevent formation of autapses(4) and allow free interaction among non-self neurons(1,2,4,5). Avoidance among self neurites is mediated by stochastic cell-surface expression of combinations of about 60 isoforms of alpha-, beta- and gamma-clustered protocadherin that provide mammalian neurons with single-cell identities(1,2,4-13). Avoidance is observed between neurons that express identical protocadherin repertoires(2,5), and single-isoform differences are sufficient to prevent self-recognition(10). Protocadherins form isoform-promiscuous cis dimers and isoform-specific homophilic trans dimers(10,14-20). Although these interactions have previously been characterized in isolation(15,17-20), structures of full-length protocadherin ectodomains have not been determined, and how these two interfaces engage in self-recognition between neuronal surfaces remains unknown. Here we determine the molecular arrangement of full-length clustered protocadherin ectodomains in single-isoform self-recognition complexes, using X-ray crystallography and cryo-electron tomography. We determine the crystal structure of the clustered protocadherin gammaB4 ectodomain, which reveals a zipper-like lattice that is formed by alternating cis and trans interactions. Using cryo-electron tomography, we show that clustered protocadherin gammaB6 ectodomains tethered to liposomes spontaneously assemble into linear arrays at membrane contact sites, in a configuration that is consistent with the assembly observed in the crystal structure. These linear assemblies pack against each other as parallel arrays to form larger two-dimensional structures between membranes. Our results suggest that the formation of ordered linear assemblies by clustered protocadherins represents the initial self-recognition step in neuronal avoidance, and thus provide support for the isoform-mismatch chain-termination model of protocadherin-mediated self-recognition, which depends on these linear chains(11). | |||
Visualization of clustered protocadherin neuronal self-recognition complexes.,Brasch J, Goodman KM, Noble AJ, Rapp M, Mannepalli S, Bahna F, Dandey VP, Bepler T, Berger B, Maniatis T, Potter CS, Carragher B, Honig B, Shapiro L Nature. 2019 Apr 10. pii: 10.1038/s41586-019-1089-3. doi:, 10.1038/s41586-019-1089-3. PMID:30971825<ref>PMID:30971825</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6e6b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cadherin 3D structures|Cadherin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Bahna F]] | |||
[[Category: Goodman KM]] | |||
[[Category: Honig B]] | |||
[[Category: Mannepalli S]] | |||
[[Category: Shapiro L]] | |||