7y9a: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7y9a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chelicerata Chelicerata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y9A FirstGlance]. <br> | <table><tr><td colspan='2'>[[7y9a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chelicerata Chelicerata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y9A 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=FUL:BETA-L-FUCOSE'>FUL</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]] 2.51Å</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=FUL:BETA-L-FUCOSE'>FUL</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=7y9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y9a OCA], [https://pdbe.org/7y9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y9a RCSB], [https://www.ebi.ac.uk/pdbsum/7y9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y9a 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=7y9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y9a OCA], [https://pdbe.org/7y9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y9a RCSB], [https://www.ebi.ac.uk/pdbsum/7y9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y9a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 13:07, 6 September 2023
Crystal structure of sDscam Ig1-2 domains, isoform beta2v6Crystal structure of sDscam Ig1-2 domains, isoform beta2v6
Structural highlights
Publication Abstract from PubMedTo create a functional neural circuit, neurons develop a molecular identity to discriminate self from non-self. The invertebrate Dscam family and vertebrate Pcdh family are implicated in determining synaptic specificity. Recently identified in Chelicerata, a shortened Dscam (sDscam) has been shown to resemble the isoform-generating characters of both Dscam and Pcdh and represent an evolutionary transition. Here we presented the molecular details of sDscam self-recognition via both trans and cis interactions using X-ray crystallographic data and functional assays. Based on our results, we proposed a molecular zipper model for the assemblies of sDscam to mediate cell-cell recognition. In this model, sDscam utilized FNIII domain to form side-by-side interactions with neighboring molecules in the same cell while established hand-in-hand interactions via Ig1 domain with molecules from another cell around. Together, our study provided a framework for understanding the assembly, recognition, and evolution of sDscam. Structural basis for the self-recognition of sDSCAM in Chelicerata.,Cheng J, Yu Y, Wang X, Zheng X, Liu T, Hu D, Jin Y, Lai Y, Fu TM, Chen Q Nat Commun. 2023 May 2;14(1):2522. doi: 10.1038/s41467-023-38205-1. PMID:37130844[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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