3ual
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/1433E_HUMAN 1433E_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. | [https://www.uniprot.org/uniprot/1433E_HUMAN 1433E_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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Myeloid leukaemia factor 1 (MLF1) binds to 14-3-3 adapter proteins by a sequence surrounding Ser34 with the functional consequences of this interaction largely unknown. We present here the high-resolution crystal structure of this binding motif [MLF1(29-42)pSer34] in complex with 14-3-3epsilon and analyse the interaction with isothermal titration calorimetry. Fragment-based ligand discovery employing crystals of the binary 14-3-3epsilon/MLF1(29-42)pSer34 complex was used to identify a molecule that binds to the interface rim of the two proteins, potentially representing the starting point for the development of a small molecule that stabilizes the MLF1/14-3-3 protein-protein interaction. Such a compound might be used as a chemical biology tool to further analyse the 14-3-3/MLF1 interaction without the use of genetic methods. Database Structural data are available in the Protein Data Bank under the accession number(s) 3UAL [14-3-3epsilon/MLF1(29-42)pSer34 complex] and 3UBW [14-3-3epsilon/MLF1(29-42)pSer34/3-pyrrolidinol complex] Structured digital abstract * 14-3-3 epsilon and MLF1 bind by x-ray crystallography (View interaction) * 14-3-3 epsilon and MLF1 bind by isothermal titration calorimetry (View Interaction: 1, 2). | ||
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| + | Structural insights of the MLF1/14-3-3 interaction.,Molzan M, Weyand M, Rose R, Ottmann C FEBS J. 2011 Dec 8. doi: 10.1111/j.1742-4658.2011.08445.x. PMID:22151054<ref>PMID:22151054</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3ual" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal Structure of 14-3-3 epsilon with Mlf1 peptide
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