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| | <StructureSection load='5szp' size='340' side='right'caption='[[5szp]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5szp' size='340' side='right'caption='[[5szp]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5szp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SZP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5SZP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5szp]] 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=5SZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SZP FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5szq|5szq]], [[5szo|5szo]], [[5szn|5szn]], [[5szm|5szm]], [[5szl|5szl]]</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>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pcdhgb7, mCG_133388 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5szp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szp OCA], [https://pdbe.org/5szp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5szp RCSB], [https://www.ebi.ac.uk/pdbsum/5szp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5szp ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5szp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szp OCA], [http://pdbe.org/5szp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5szp RCSB], [http://www.ebi.ac.uk/pdbsum/5szp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5szp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q91XX3_MOUSE Q91XX3_MOUSE]] Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.[SAAS:SAAS00348345] | + | [https://www.uniprot.org/uniprot/Q91XX3_MOUSE Q91XX3_MOUSE] Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.[SAAS:SAAS00348345] |
| | <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: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Bahna, F]] | + | [[Category: Bahna F]] |
| - | [[Category: Goodman, K M]] | + | [[Category: Goodman KM]] |
| - | [[Category: Honig, B]] | + | [[Category: Honig B]] |
| - | [[Category: Mannepalli, S]] | + | [[Category: Mannepalli S]] |
| - | [[Category: Shapiro, L]] | + | [[Category: Shapiro L]] |
| - | [[Category: Cell adhesion]]
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| Structural highlights
Function
Q91XX3_MOUSE Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.[SAAS:SAAS00348345]
Publication Abstract from PubMed
Stochastic cell-surface expression of alpha-, beta-, and gamma-clustered protocadherins (Pcdhs) provides vertebrate neurons with single-cell identities that underlie neuronal self-recognition. Here we report crystal structures of ectodomain fragments comprising cell-cell recognition regions of mouse gamma-Pcdhs gammaA1, gammaA8, gammaB2, and gammaB7 revealing trans-homodimers, and of C-terminal ectodomain fragments from gamma-Pcdhs gammaA4 and gammaB2, which depict cis-interacting regions in monomeric form. Together these structures span the entire gamma-Pcdh ectodomain. The trans-dimer structures reveal determinants of gamma-Pcdh isoform-specific homophilic recognition. We identified and structurally mapped cis-dimerization mutations to the C-terminal ectodomain structures. Biophysical studies showed that Pcdh ectodomains from gammaB-subfamily isoforms formed cis dimers, whereas gammaA isoforms did not, but both gammaA and gammaB isoforms could interact in cis with alpha-Pcdhs. Together, these data show how interaction specificity is distributed over all domains of the gamma-Pcdh trans interface, and suggest that subfamily- or isoform-specific cis-interactions may play a role in the Pcdh-mediated neuronal self-recognition code.
gamma-Protocadherin structural diversity and functional implications.,Goodman KM, Rubinstein R, Thu CA, Mannepalli S, Bahna F, Ahlsen G, Rittenhouse C, Maniatis T, Honig B, Shapiro L Elife. 2016 Oct 26;5. pii: e20930. doi: 10.7554/eLife.20930. PMID:27782885[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goodman KM, Rubinstein R, Thu CA, Mannepalli S, Bahna F, Ahlsen G, Rittenhouse C, Maniatis T, Honig B, Shapiro L. gamma-Protocadherin structural diversity and functional implications. Elife. 2016 Oct 26;5. pii: e20930. doi: 10.7554/eLife.20930. PMID:27782885 doi:http://dx.doi.org/10.7554/eLife.20930
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