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| | <StructureSection load='4zi9' size='340' side='right'caption='[[4zi9]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4zi9' size='340' side='right'caption='[[4zi9]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zi9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZI9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zi9]] 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=4ZI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZI9 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></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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zi8|4zi8]]</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></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=4zi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zi9 OCA], [http://pdbe.org/4zi9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zi9 RCSB], [http://www.ebi.ac.uk/pdbsum/4zi9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zi9 ProSAT]</span></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=4zi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zi9 OCA], [https://pdbe.org/4zi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zi9 RCSB], [https://www.ebi.ac.uk/pdbsum/4zi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zi9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q91XZ0_MOUSE Q91XZ0_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/Q91XZ0_MOUSE Q91XZ0_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: Gaudet, R]] | + | [[Category: Mus musculus]] |
| - | [[Category: Lau, S Y]] | + | [[Category: Gaudet R]] |
| - | [[Category: Marks, D S]] | + | [[Category: Lau S-Y]] |
| - | [[Category: Nicoludis, J M]] | + | [[Category: Marks DS]] |
| - | [[Category: Scharfe, C P.I]] | + | [[Category: Nicoludis JM]] |
| - | [[Category: Weihofen, W A]] | + | [[Category: Scharfe CPI]] |
| - | [[Category: Cell adhesion]]
| + | [[Category: Weihofen WA]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Membrane protein]]
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| - | [[Category: Protocadherin]]
| + | |
| Structural highlights
Function
Q91XZ0_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
Clustered protocadherin (Pcdh) proteins mediate dendritic self-avoidance in neurons via specific homophilic interactions in their extracellular cadherin (EC) domains. We determined crystal structures of EC1-EC3, containing the homophilic specificity-determining region, of two mouse clustered Pcdh isoforms (PcdhgammaA1 and PcdhgammaC3) to investigate the nature of the homophilic interaction. Within the crystal lattices, we observe antiparallel interfaces consistent with a role in trans cell-cell contact. Antiparallel dimerization is supported by evolutionary correlations. Two interfaces, located primarily on EC2-EC3, involve distinctive clustered Pcdh structure and sequence motifs, lack predicted glycosylation sites, and contain residues highly conserved in orthologs but not paralogs, pointing toward their biological significance as homophilic interaction interfaces. These two interfaces are similar yet distinct, reflecting a possible difference in interaction architecture between clustered Pcdh subfamilies. These structures initiate a molecular understanding of clustered Pcdh assemblies that are required to produce functional neuronal networks.
Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity.,Nicoludis JM, Lau SY, Scharfe CP, Marks DS, Weihofen WA, Gaudet R Structure. 2015 Nov 3;23(11):2087-98. doi: 10.1016/j.str.2015.09.005. Epub 2015, Oct 15. PMID:26481813[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nicoludis JM, Lau SY, Scharfe CP, Marks DS, Weihofen WA, Gaudet R. Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity. Structure. 2015 Nov 3;23(11):2087-98. doi: 10.1016/j.str.2015.09.005. Epub 2015, Oct 15. PMID:26481813 doi:http://dx.doi.org/10.1016/j.str.2015.09.005
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