6nrq: Difference between revisions
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==Crystal structure of Dpr10 IG1 bound to DIP-alpha IG1== | |||
<StructureSection load='6nrq' size='340' side='right'caption='[[6nrq]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nrq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NRQ 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]] 1.8Å</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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6nrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nrq OCA], [https://pdbe.org/6nrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nrq RCSB], [https://www.ebi.ac.uk/pdbsum/6nrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nrq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9VT83_DROME Q9VT83_DROME] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In stereotyped neuronal networks, synaptic connectivity is dictated by cell surface proteins, which assign unique identities to neurons, and physically mediate axon guidance and synapse targeting. We recently identified two groups of immunoglobulin superfamily proteins in Drosophila, Dprs and DIPs, as strong candidates for synapse targeting functions. Here, we uncover the molecular basis of specificity in Dpr-DIP mediated cellular adhesions and neuronal connectivity. First, we present five crystal structures of Dpr-DIP and DIP-DIP complexes, highlighting the evolutionary and structural origins of diversification in Dpr and DIP proteins and their interactions. We further show that structures can be used to rationally engineer receptors with novel specificities or modified affinities, which can be used to study specific circuits that require Dpr-DIP interactions to help establish connectivity. We investigate one pair, engineered Dpr10 and DIP-alpha, for function in the neuromuscular circuit in flies, and reveal roles for homophilic and heterophilic binding in wiring. | |||
Molecular basis of synaptic specificity by immunoglobulin superfamily receptors in Drosophila.,Cheng S, Ashley J, Kurleto JD, Lobb-Rabe M, Park YJ, Carrillo RA, Ozkan E Elife. 2019 Jan 28;8. pii: 41028. doi: 10.7554/eLife.41028. PMID:30688651<ref>PMID:30688651</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Cheng | <div class="pdbe-citations 6nrq" style="background-color:#fffaf0;"></div> | ||
[[Category: Kurleto | == References == | ||
[[Category: Park | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Large Structures]] | |||
[[Category: Cheng S]] | |||
[[Category: Kurleto JD]] | |||
[[Category: Ozkan E]] | |||
[[Category: Park YJ]] | |||
Latest revision as of 09:58, 11 October 2023
Crystal structure of Dpr10 IG1 bound to DIP-alpha IG1Crystal structure of Dpr10 IG1 bound to DIP-alpha IG1
Structural highlights
FunctionPublication Abstract from PubMedIn stereotyped neuronal networks, synaptic connectivity is dictated by cell surface proteins, which assign unique identities to neurons, and physically mediate axon guidance and synapse targeting. We recently identified two groups of immunoglobulin superfamily proteins in Drosophila, Dprs and DIPs, as strong candidates for synapse targeting functions. Here, we uncover the molecular basis of specificity in Dpr-DIP mediated cellular adhesions and neuronal connectivity. First, we present five crystal structures of Dpr-DIP and DIP-DIP complexes, highlighting the evolutionary and structural origins of diversification in Dpr and DIP proteins and their interactions. We further show that structures can be used to rationally engineer receptors with novel specificities or modified affinities, which can be used to study specific circuits that require Dpr-DIP interactions to help establish connectivity. We investigate one pair, engineered Dpr10 and DIP-alpha, for function in the neuromuscular circuit in flies, and reveal roles for homophilic and heterophilic binding in wiring. Molecular basis of synaptic specificity by immunoglobulin superfamily receptors in Drosophila.,Cheng S, Ashley J, Kurleto JD, Lobb-Rabe M, Park YJ, Carrillo RA, Ozkan E Elife. 2019 Jan 28;8. pii: 41028. doi: 10.7554/eLife.41028. PMID:30688651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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