6vft: Difference between revisions
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==Crystal structure of human delta protocadherin 17 EC1-EC4== | |||
<StructureSection load='6vft' size='340' side='right'caption='[[6vft]], [[Resolution|resolution]] 3.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6vft]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VFT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.71Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vft OCA], [https://pdbe.org/6vft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vft RCSB], [https://www.ebi.ac.uk/pdbsum/6vft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vft ProSAT]</span></td></tr> | |||
</table> | |||
<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 6vft" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cadherin 3D structures|Cadherin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Brasch J]] | |||
[[Category: Harrison OJ]] | |||
[[Category: Shapiro L]] | |||
Latest revision as of 11:25, 17 October 2024
Crystal structure of human delta protocadherin 17 EC1-EC4Crystal structure of human delta protocadherin 17 EC1-EC4
Structural highlights
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. See AlsoReferences
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