6eg0: Difference between revisions

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<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=6eg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eg0 OCA], [http://pdbe.org/6eg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eg0 RCSB], [http://www.ebi.ac.uk/pdbsum/6eg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eg0 ProSAT]</span></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=6eg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eg0 OCA], [http://pdbe.org/6eg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eg0 RCSB], [http://www.ebi.ac.uk/pdbsum/6eg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eg0 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Binding between DIP and Dpr neuronal recognition proteins has been proposed to regulate synaptic connections between lamina and medulla neurons in the Drosophila visual system. Each lamina neuron was previously shown to express many Dprs. Here, we demonstrate, by contrast, that their synaptic partners typically express one or two DIPs, with binding specificities matched to the lamina neuron-expressed Dprs. A deeper understanding of the molecular logic of DIP/Dpr interaction requires quantitative studies on the properties of these proteins. We thus generated a quantitative affinity-based DIP/Dpr interactome for all DIP/Dpr protein family members. This revealed a broad range of affinities and identified homophilic binding for some DIPs and some Dprs. These data, along with full-length ectodomain DIP/Dpr and DIP/DIP crystal structures, led to the identification of molecular determinants of DIP/Dpr specificity. This structural knowledge, along with a comprehensive set of quantitative binding affinities, provides new tools for functional studies in vivo.
Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins.,Cosmanescu F, Katsamba PS, Sergeeva AP, Ahlsen G, Patel SD, Brewer JJ, Tan L, Xu S, Xiao Q, Nagarkar-Jaiswal S, Nern A, Bellen HJ, Zipursky SL, Honig B, Shapiro L Neuron. 2018 Nov 12. pii: S0896-6273(18)30954-1. doi:, 10.1016/j.neuron.2018.10.046. PMID:30467080<ref>PMID:30467080</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6eg0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>

Revision as of 11:52, 19 December 2018

Crystal stucture of Dpr4 Ig1-Ig2 in complex with DIP-Eta Ig1-Ig3Crystal stucture of Dpr4 Ig1-Ig2 in complex with DIP-Eta Ig1-Ig3

Structural highlights

6eg0 is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , ,
Gene:dpr4, CG12593, CG14707, CT34497, Dmel\CG33512, Dpr-4, Dpr4, dpr4-RA, CG33512, Dmel_CG33512 (DROME), DIP-eta, 14010, CT33567, Dmel\CG14010, CG14010, Dmel_CG14010 (DROME)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Binding between DIP and Dpr neuronal recognition proteins has been proposed to regulate synaptic connections between lamina and medulla neurons in the Drosophila visual system. Each lamina neuron was previously shown to express many Dprs. Here, we demonstrate, by contrast, that their synaptic partners typically express one or two DIPs, with binding specificities matched to the lamina neuron-expressed Dprs. A deeper understanding of the molecular logic of DIP/Dpr interaction requires quantitative studies on the properties of these proteins. We thus generated a quantitative affinity-based DIP/Dpr interactome for all DIP/Dpr protein family members. This revealed a broad range of affinities and identified homophilic binding for some DIPs and some Dprs. These data, along with full-length ectodomain DIP/Dpr and DIP/DIP crystal structures, led to the identification of molecular determinants of DIP/Dpr specificity. This structural knowledge, along with a comprehensive set of quantitative binding affinities, provides new tools for functional studies in vivo.

Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins.,Cosmanescu F, Katsamba PS, Sergeeva AP, Ahlsen G, Patel SD, Brewer JJ, Tan L, Xu S, Xiao Q, Nagarkar-Jaiswal S, Nern A, Bellen HJ, Zipursky SL, Honig B, Shapiro L Neuron. 2018 Nov 12. pii: S0896-6273(18)30954-1. doi:, 10.1016/j.neuron.2018.10.046. PMID:30467080[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Cosmanescu F, Katsamba PS, Sergeeva AP, Ahlsen G, Patel SD, Brewer JJ, Tan L, Xu S, Xiao Q, Nagarkar-Jaiswal S, Nern A, Bellen HJ, Zipursky SL, Honig B, Shapiro L. Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins. Neuron. 2018 Nov 12. pii: S0896-6273(18)30954-1. doi:, 10.1016/j.neuron.2018.10.046. PMID:30467080 doi:http://dx.doi.org/10.1016/j.neuron.2018.10.046

6eg0, resolution 2.90Å

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