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4hkc
From Proteopedia
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| - | {{STRUCTURE_4hkc| PDB=4hkc | SCENE= }} | ||
| - | ===14-3-3-zeta in complex with S1011 phosphorylated integrin alpha-4 peptide=== | ||
| - | {{ABSTRACT_PUBMED_23763993}} | ||
| - | == | + | ==14-3-3-zeta in complex with S1011 phosphorylated integrin alpha-4 peptide== |
| - | [[http://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN | + | <StructureSection load='4hkc' size='340' side='right'caption='[[4hkc]], [[Resolution|resolution]] 2.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hkc]] is a 2 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=4HKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HKC FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=4hkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hkc OCA], [https://pdbe.org/4hkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hkc RCSB], [https://www.ebi.ac.uk/pdbsum/4hkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hkc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN] 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.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Integrins are a family of heterodimeric (alpha+beta) adhesion receptors that play key roles in many cellular processes. Integrins are unusual in that their functions can be modulated from both outside and inside the cell. Inside-out signaling is mediated by binding adaptor proteins to the flexible cytoplasmic tails of the alpha- and beta-integrin subunits. Talin is one well-known intracellular activator, but various other adaptors bind to integrin tails, including 14-3-3-zeta, a member of the 14-3-3 family of dimeric proteins that have a preference for binding phosphorylated sequence motifs. Phosphorylation of a threonine in the beta2 integrin tail has been shown to modulate beta2/14-3-3-zeta interactions, and recently, the alpha4 integrin tail was reported to bind to 14-3-3-zeta and associate with paxillin in a ternary complex that is regulated by serine phosphorylation. Here, we use a range of biophysical techniques to characterize interactions between 14-3-3-zeta and the cytoplasmic tails of alpha4, beta1, beta2 and beta3 integrins. The X-ray structure of the 14-3-3-zeta/alpha4 complex indicates a canonical binding mode for the alpha4 phospho-peptide, but unexpected features are also observed: residues outside the consensus 14-3-3-zeta binding motif are shown to be essential for an efficient interaction; in contrast, a short beta2 phospho-peptide is sufficient for high-affinity binding to 14-3-3-zeta. In addition, we report novel 14-3-3-zeta/integrin tail interactions that are independent of phosphorylation. Of the integrin tails studied, the strongest interaction with 14-3-3-zeta is observed for the beta1A variant. In summary, new insights about 14-3-3-zeta/integrin tail interactions that have implications for the role of these molecular associations in cells are described. | ||
| - | + | Characterization of 14-3-3-zeta Interactions with Integrin Tails.,Bonet R, Vakonakis I, Campbell ID J Mol Biol. 2013 Jun 11. pii: S0022-2836(13)00354-9. doi:, 10.1016/j.jmb.2013.05.024. PMID:23763993<ref>PMID:23763993</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | + | <div class="pdbe-citations 4hkc" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | [[ | + | ==See Also== |
| - | + | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Bonet R]] | ||
| + | [[Category: Campbell ID]] | ||
Current revision
14-3-3-zeta in complex with S1011 phosphorylated integrin alpha-4 peptide
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