|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5dzx' size='340' side='right'caption='[[5dzx]], [[Resolution|resolution]] 2.88Å' scene=''> | | <StructureSection load='5dzx' size='340' side='right'caption='[[5dzx]], [[Resolution|resolution]] 2.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dzx]] 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=5DZX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DZX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dzx]] 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=5DZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DZX FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.879Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dzv|5dzv]], [[5dzw|5dzw]], [[5dzy|5dzy]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pcdhb6 ([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=5dzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dzx OCA], [https://pdbe.org/5dzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dzx RCSB], [https://www.ebi.ac.uk/pdbsum/5dzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dzx 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=5dzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dzx OCA], [http://pdbe.org/5dzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dzx RCSB], [http://www.ebi.ac.uk/pdbsum/5dzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dzx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PCDB6_MOUSE PCDB6_MOUSE] Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (PubMed:27161523). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain (PubMed:27161523).<ref>PMID:27161523</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 24: |
| | </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: Cadherin]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Extracellular]]
| + | |
| Structural highlights
5dzx is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.879Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PCDB6_MOUSE Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (PubMed:27161523). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain (PubMed:27161523).[1]
Publication Abstract from PubMed
Clustered protocadherin proteins (alpha-, beta-, and gamma-Pcdhs) provide a high level of cell-surface diversity to individual vertebrate neurons, engaging in highly specific homophilic interactions to mediate important roles in mammalian neural circuit development. How Pcdhs bind homophilically through their extracellular cadherin (EC) domains among dozens of highly similar isoforms has not been determined. Here, we report crystal structures for extracellular regions from four mouse Pcdh isoforms (alpha4, alpha7, beta6, and beta8), revealing a canonical head-to-tail interaction mode for homophilic trans dimers comprising primary intermolecular EC1:EC4 and EC2:EC3 interactions. A subset of trans interface residues exhibit isoform-specific conservation, suggesting roles in recognition specificity. Mutation of these residues, along with trans-interacting partner residues, altered the specificities of Pcdh interactions. Together, these data show how sequence variation among Pcdh isoforms encodes their diverse strict homophilic recognition specificities, which are required for their key roles in neural circuit assembly.
Structural Basis of Diverse Homophilic Recognition by Clustered alpha- and beta-Protocadherins.,Goodman KM, Rubinstein R, Thu CA, Bahna F, Mannepalli S, Ahlsen G, Rittenhouse C, Maniatis T, Honig B, Shapiro L Neuron. 2016 May 18;90(4):709-23. doi: 10.1016/j.neuron.2016.04.004. Epub 2016, May 5. PMID:27161523[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goodman KM, Rubinstein R, Thu CA, Bahna F, Mannepalli S, Ahlsen G, Rittenhouse C, Maniatis T, Honig B, Shapiro L. Structural Basis of Diverse Homophilic Recognition by Clustered alpha- and beta-Protocadherins. Neuron. 2016 May 18;90(4):709-23. doi: 10.1016/j.neuron.2016.04.004. Epub 2016, May 5. PMID:27161523 doi:http://dx.doi.org/10.1016/j.neuron.2016.04.004
- ↑ Goodman KM, Rubinstein R, Thu CA, Bahna F, Mannepalli S, Ahlsen G, Rittenhouse C, Maniatis T, Honig B, Shapiro L. Structural Basis of Diverse Homophilic Recognition by Clustered alpha- and beta-Protocadherins. Neuron. 2016 May 18;90(4):709-23. doi: 10.1016/j.neuron.2016.04.004. Epub 2016, May 5. PMID:27161523 doi:http://dx.doi.org/10.1016/j.neuron.2016.04.004
|
