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| | <StructureSection load='4zps' size='340' side='right'caption='[[4zps]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='4zps' size='340' side='right'caption='[[4zps]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zps]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZPS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zps]] is a 1 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=4ZPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZPS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zpl|4zpl]], [[4zpm|4zpm]], [[4zpn|4zpn]], [[4zpo|4zpo]], [[4zpp|4zpp]], [[4zpq|4zpq]]</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=4zps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zps OCA], [https://pdbe.org/4zps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zps RCSB], [https://www.ebi.ac.uk/pdbsum/4zps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zps ProSAT]</span></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=4zps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zps OCA], [http://pdbe.org/4zps PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zps RCSB], [http://www.ebi.ac.uk/pdbsum/4zps PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zps ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q91XY0_MOUSE Q91XY0_MOUSE]] Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.[SAAS:SAAS00311819] | + | [https://www.uniprot.org/uniprot/Q91XY0_MOUSE Q91XY0_MOUSE] Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.[SAAS:SAAS00311819] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Goodman, K M]] | + | [[Category: Mus musculus]] |
| - | [[Category: Mannepalli, S]] | + | [[Category: Goodman KM]] |
| - | [[Category: Shapiro, L]] | + | [[Category: Mannepalli S]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Shapiro L]] |
| Structural highlights
Function
Q91XY0_MOUSE Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.[SAAS:SAAS00311819]
Publication Abstract from PubMed
Self-avoidance, a process preventing interactions of axons and dendrites from the same neuron during development, is mediated in vertebrates through the stochastic single-neuron expression of clustered protocadherin protein isoforms. Extracellular cadherin (EC) domains mediate isoform-specific homophilic binding between cells, conferring cell recognition through a poorly understood mechanism. Here, we report crystal structures for the EC1-EC3 domain regions from four protocadherin isoforms representing the alpha, beta, and gamma subfamilies. All are rod shaped and monomeric in solution. Biophysical measurements, cell aggregation assays, and computational docking reveal that trans binding between cells depends on the EC1-EC4 domains, which interact in an antiparallel orientation. We also show that the EC6 domains are required for the formation of cis-dimers. Overall, our results are consistent with a model in which protocadherin cis-dimers engage in a head-to-tail interaction between EC1-EC4 domains from apposed cell surfaces, possibly forming a zipper-like protein assembly, and thus providing a size-dependent self-recognition mechanism.
Molecular Logic of Neuronal Self-Recognition through Protocadherin Domain Interactions.,Rubinstein R, Thu CA, Goodman KM, Wolcott HN, Bahna F, Mannepalli S, Ahlsen G, Chevee M, Halim A, Clausen H, Maniatis T, Shapiro L, Honig B Cell. 2015 Oct 22;163(3):629-42. doi: 10.1016/j.cell.2015.09.026. Epub 2015 Oct, 17. PMID:26478182[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rubinstein R, Thu CA, Goodman KM, Wolcott HN, Bahna F, Mannepalli S, Ahlsen G, Chevee M, Halim A, Clausen H, Maniatis T, Shapiro L, Honig B. Molecular Logic of Neuronal Self-Recognition through Protocadherin Domain Interactions. Cell. 2015 Oct 22;163(3):629-42. doi: 10.1016/j.cell.2015.09.026. Epub 2015 Oct, 17. PMID:26478182 doi:http://dx.doi.org/10.1016/j.cell.2015.09.026
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