5f67: Difference between revisions
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<StructureSection load='5f67' size='340' side='right'caption='[[5f67]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='5f67' size='340' side='right'caption='[[5f67]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5f67]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5f67]] 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=5F67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F67 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5f67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f67 OCA], [https://pdbe.org/5f67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f67 RCSB], [https://www.ebi.ac.uk/pdbsum/5f67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f67 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/INAD_DROME INAD_DROME] Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex.<ref>PMID:7826638</ref> <ref>PMID:11342563</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Liu | [[Category: Liu W]] | ||
[[Category: Shang | [[Category: Shang Y]] | ||
[[Category: Ye | [[Category: Ye F]] | ||
[[Category: Zhang | [[Category: Zhang M]] | ||
Latest revision as of 09:39, 19 July 2023
An exquisitely specific PDZ/target recognition revealed by the structure of INAD PDZ3 in complex with TRP channel tailAn exquisitely specific PDZ/target recognition revealed by the structure of INAD PDZ3 in complex with TRP channel tail
Structural highlights
FunctionINAD_DROME Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex.[1] [2] Publication Abstract from PubMedThe vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target proteins with modest binding affinities and specificities. Such promiscuous PDZ/target interactions are not compatible with highly specific physiological functions of PDZ domain proteins and their targets. Here, we report an unexpected PDZ/target binding occurring between the scaffold protein inactivation no afterpotential D (INAD) and transient receptor potential (TRP) channel in Drosophila photoreceptors. The C-terminal 15 residues of TRP are required for the specific interaction with INAD PDZ3. The INAD PDZ3/TRP peptide complex structure reveals that only the extreme C-terminal Leu of TRP binds to the canonical alphaB/betaB groove of INAD PDZ3. The rest of the TRP peptide, by forming a beta hairpin structure, binds to a surface away from the alphaB/betaB groove of PDZ3 and contributes to the majority of the binding energy. Thus, the INAD PDZ3/TRP channel interaction is exquisitely specific and represents a new mode of PDZ/target recognitions. An Exquisitely Specific PDZ/Target Recognition Revealed by the Structure of INAD PDZ3 in Complex with TRP Channel Tail.,Ye F, Liu W, Shang Y, Zhang M Structure. 2016 Jan 27. pii: S0969-2126(16)00006-X. doi:, 10.1016/j.str.2015.12.013. PMID:26853938[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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