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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 [http://en.wikipedia.org/wiki/Drome Drome]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5F67 FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">inaD, CG3504 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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]] 1.76Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f67 OCA], [http://pdbe.org/5f67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f67 RCSB], [http://www.ebi.ac.uk/pdbsum/5f67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f67 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=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 == |
| - | [[http://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> | + | [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: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, W]] | + | [[Category: Liu W]] |
| - | [[Category: Shang, Y]] | + | [[Category: Shang Y]] |
| - | [[Category: Ye, F]] | + | [[Category: Ye F]] |
| - | [[Category: Zhang, M]] | + | [[Category: Zhang M]] |
| - | [[Category: Atypical]]
| + | |
| - | [[Category: Inad]]
| + | |
| - | [[Category: Pdz]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Trp]]
| + | |
| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
The 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
- ↑ Shieh BH, Niemeyer B. A novel protein encoded by the InaD gene regulates recovery of visual transduction in Drosophila. Neuron. 1995 Jan;14(1):201-10. PMID:7826638
- ↑ Kumar R, Shieh BH. The second PDZ domain of INAD is a type I domain involved in binding to eye protein kinase C. Mutational analysis and naturally occurring variants. J Biol Chem. 2001 Jul 6;276(27):24971-7. Epub 2001 May 7. PMID:11342563 doi:http://dx.doi.org/10.1074/jbc.M103570200
- ↑ Ye F, Liu W, Shang Y, Zhang M. An Exquisitely Specific PDZ/Target Recognition Revealed by the Structure of INAD PDZ3 in Complex with TRP Channel Tail. Structure. 2016 Jan 27. pii: S0969-2126(16)00006-X. doi:, 10.1016/j.str.2015.12.013. PMID:26853938 doi:http://dx.doi.org/10.1016/j.str.2015.12.013
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