5yqg
From Proteopedia
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==The structure of 14-3-3 and pNumb peptide== | ==The structure of 14-3-3 and pNumb peptide== | ||
| - | <StructureSection load='5yqg' size='340' side='right' caption='[[5yqg]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5yqg' size='340' side='right'caption='[[5yqg]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5yqg]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YQG OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5yqg]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YQG 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]] 2.1Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=5yqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yqg OCA], [https://pdbe.org/5yqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yqg RCSB], [https://www.ebi.ac.uk/pdbsum/5yqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yqg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/1433F_MOUSE 1433F_MOUSE] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Traffic of cargo across membranes helps establish, maintain, and reorganize distinct cellular compartments and is fundamental to many metabolic processes. The cargo-selective endocytic adaptor Numb participates in clathrin-dependent endocytosis by attaching cargoes to the clathrin adaptor alpha-adaptin. The phosphorylation of Numb at Ser(265) and Ser(284) recruits the regulatory protein 14-3-3, accompanied by the dissociation of Numb from alpha-adaptin and Numb's translocation from the cortical membrane to the cytosol. However, the molecular mechanisms underlying the Numb-alpha-adaptin interaction and its regulation by Numb phosphorylation and 14-3-3 recruitment remain poorly understood. Here, biochemical and structural analyses of the Numb.14-3-3 complex revealed that Numb phosphorylation at both Ser(265) and Ser(284) is required for Numb's efficient interaction with 14-3-3. We also discovered that an RQFRF motif surrounding Ser(265) in Numb functions together with the canonical C-terminal DPF motif, required for Numb's interaction with alpha-adaptin, to form a stable complex with alpha-adaptin. Of note, we provide evidence that the phosphorylation-induced binding of 14-3-3 to Numb directly competes with the binding of alpha-adaptin to Numb. Our findings suggest a potential mechanism governing the dynamic assembly of Numb with alpha-adaptin or 14-3-3. This dual-site recognition of Numb by alpha-adaptin may have implications for other alpha-adaptin targets. We propose that the newly identified alpha-adaptin-binding site surrounding Ser(265) in Numb functions as a triggering mechanism for the dynamic dissociation of the Numb.alpha-adaptin complex. | ||
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| + | Structural determinants controlling 14-3-3 recruitment to the endocytic adaptor Numb and dissociation of the Numb.alpha-adaptin complex.,Chen X, Liu Z, Shan Z, Yao W, Gu A, Wen W J Biol Chem. 2018 Mar 16;293(11):4149-4158. doi: 10.1074/jbc.RA117.000897. Epub, 2018 Jan 30. PMID:29382713<ref>PMID:29382713</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5yqg" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: | + | [[Category: Chen X]] |
| - | [[Category: | + | [[Category: Liu Z]] |
| - | [[Category: | + | [[Category: Wen W]] |
| - | + | ||
| - | + | ||
Current revision
The structure of 14-3-3 and pNumb peptide
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Categories: Large Structures | Mus musculus | Chen X | Liu Z | Wen W
