6vg4: Difference between revisions
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==human protocadherin 10 ectodomain== | |||
<StructureSection load='6vg4' size='340' side='right'caption='[[6vg4]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6vg4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VG4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <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=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=6vg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vg4 OCA], [http://pdbe.org/6vg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vg4 RCSB], [http://www.ebi.ac.uk/pdbsum/6vg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vg4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PCD10_HUMAN PCD10_HUMAN]] Potential calcium-dependent cell-adhesion protein. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Non-clustered delta1- and delta2-protocadherins, close relatives of clustered protocadherins, function in cell adhesion and motility and play essential roles in neural patterning. To understand the molecular interactions underlying these functions, we used solution biophysics to characterize binding of delta1- and delta2-protocadherins, determined crystal structures of ectodomain complexes from each family, and assessed ectodomain assembly in reconstituted intermembrane junctions by cryoelectron tomography (cryo-ET). Homophilic trans (cell-cell) interactions were preferred for all delta-protocadherins, with additional weaker heterophilic interactions observed exclusively within each subfamily. As expected, delta1- and delta2-protocadherin trans dimers formed through antiparallel EC1-EC4 interfaces, like clustered protocadherins. However, no ectodomain-mediated cis (same-cell) interactions were detectable in solution; consistent with this, cryo-ET of reconstituted junctions revealed dense assemblies lacking the characteristic order observed for clustered protocadherins. Our results define non-clustered protocadherin binding properties and their structural basis, providing a foundation for interpreting their functional roles in neural patterning. | |||
Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered delta-Protocadherins.,Harrison OJ, Brasch J, Katsamba PS, Ahlsen G, Noble AJ, Dan H, Sampogna RV, Potter CS, Carragher B, Honig B, Shapiro L Cell Rep. 2020 Feb 25;30(8):2655-2671.e7. doi: 10.1016/j.celrep.2020.02.003. PMID:32101743<ref>PMID:32101743</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6vg4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Brasch, J]] | |||
[[Category: Harrison, O J]] | |||
[[Category: Shapiro, L]] | |||
[[Category: Cadherin]] | |||
[[Category: Calcium binding]] | |||
[[Category: Cell adhesion]] | |||
[[Category: Non-clustered]] | |||
[[Category: Protocadherin]] | |||
Revision as of 10:31, 11 March 2020
human protocadherin 10 ectodomainhuman protocadherin 10 ectodomain
Structural highlights
Function[PCD10_HUMAN] Potential calcium-dependent cell-adhesion protein. Publication Abstract from PubMedNon-clustered delta1- and delta2-protocadherins, close relatives of clustered protocadherins, function in cell adhesion and motility and play essential roles in neural patterning. To understand the molecular interactions underlying these functions, we used solution biophysics to characterize binding of delta1- and delta2-protocadherins, determined crystal structures of ectodomain complexes from each family, and assessed ectodomain assembly in reconstituted intermembrane junctions by cryoelectron tomography (cryo-ET). Homophilic trans (cell-cell) interactions were preferred for all delta-protocadherins, with additional weaker heterophilic interactions observed exclusively within each subfamily. As expected, delta1- and delta2-protocadherin trans dimers formed through antiparallel EC1-EC4 interfaces, like clustered protocadherins. However, no ectodomain-mediated cis (same-cell) interactions were detectable in solution; consistent with this, cryo-ET of reconstituted junctions revealed dense assemblies lacking the characteristic order observed for clustered protocadherins. Our results define non-clustered protocadherin binding properties and their structural basis, providing a foundation for interpreting their functional roles in neural patterning. Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered delta-Protocadherins.,Harrison OJ, Brasch J, Katsamba PS, Ahlsen G, Noble AJ, Dan H, Sampogna RV, Potter CS, Carragher B, Honig B, Shapiro L Cell Rep. 2020 Feb 25;30(8):2655-2671.e7. doi: 10.1016/j.celrep.2020.02.003. PMID:32101743[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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