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| | <StructureSection load='6px0' size='340' side='right'caption='[[6px0]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='6px0' size='340' side='right'caption='[[6px0]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6px0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PX0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PX0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6px0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PX0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 1.55Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIPL1, AIPL2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=6px0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6px0 OCA], [http://pdbe.org/6px0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6px0 RCSB], [http://www.ebi.ac.uk/pdbsum/6px0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6px0 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=6px0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6px0 OCA], [https://pdbe.org/6px0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6px0 RCSB], [https://www.ebi.ac.uk/pdbsum/6px0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6px0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/AIPL1_HUMAN AIPL1_HUMAN]] Leber congenital amaurosis;Cone rod dystrophy. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/AIPL1_HUMAN AIPL1_HUMAN] Leber congenital amaurosis;Cone rod dystrophy. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AIPL1_HUMAN AIPL1_HUMAN]] May be important in protein trafficking and/or protein folding and stabilization. | + | [https://www.uniprot.org/uniprot/AIPL1_HUMAN AIPL1_HUMAN] May be important in protein trafficking and/or protein folding and stabilization. |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Artemyev, N O]] | + | [[Category: Artemyev NO]] |
| - | [[Category: Yadav, R P]] | + | [[Category: Yadav RP]] |
| - | [[Category: Aipl1 tpr]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Disease
AIPL1_HUMAN Leber congenital amaurosis;Cone rod dystrophy. The disease is caused by mutations affecting the gene represented in this entry.
Function
AIPL1_HUMAN May be important in protein trafficking and/or protein folding and stabilization.
Publication Abstract from PubMed
Phosphodiesterase-6 (PDE6) is key to both phototransduction and health of rods and cones. Proper folding of PDE6 relies on the chaperone activity of aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1), and mutations in both PDE6 and AIPL1 can cause a severe form of blindness. Although AIPL1 and PDE6 are known to interact via the FK506-binding protein domain of AIPL1, the contribution of the tetratricopeptide repeat (TPR) domain of AIPL1 to its chaperone function is poorly understood. Here, we demonstrate that AIPL1-TPR interacts specifically with the regulatory Pgamma subunit of PDE6. Use of NMR chemical shift perturbation (CSP) mapping technique revealed the interface between the C-terminal portion of Pgamma and AIPL1-TPR. Our solution of the crystal structure of the AIPL1-TPR domain provided additional information, which together with the CSP data enabled us to generate a model of this interface. Biochemical analysis of chimeric AIPL1-AIP proteins supported this model and also revealed a correlation between the affinity of AIPL1-TPR for Pgamma and the ability of Pgamma to potentiate the chaperone activity of AIPL1. Based on these results, we present a model of the larger AIPL1-PDE6 complex. This supports the importance of simultaneous interactions of AIPL1-FK506-binding protein with the prenyl moieties of PDE6 and AIPL1-TPR with the Pgamma subunit during the folding and/or assembly of PDE6. This study sheds new light on the versatility of TPR domains in protein folding by describing a novel TPR-protein binding partner, Pgamma, and revealing that this subunit imparts AIPL1 selectivity for its client.
Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor-interacting protein-like 1 with the regulatory Pgamma subunit of phosphodiesterase 6.,Yadav RP, Boyd K, Yu L, Artemyev NO J Biol Chem. 2019 Oct 25;294(43):15795-15807. doi: 10.1074/jbc.RA119.010666. Epub, 2019 Sep 5. PMID:31488544[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yadav RP, Boyd K, Yu L, Artemyev NO. Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor-interacting protein-like 1 with the regulatory Pgamma subunit of phosphodiesterase 6. J Biol Chem. 2019 Oct 25;294(43):15795-15807. doi: 10.1074/jbc.RA119.010666. Epub, 2019 Sep 5. PMID:31488544 doi:http://dx.doi.org/10.1074/jbc.RA119.010666
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