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3ual

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<StructureSection load='3ual' size='340' side='right'caption='[[3ual]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3ual' size='340' side='right'caption='[[3ual]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ual]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ual]] 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=3UAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2br9|2br9]], [[3ubw|3ubw]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YWHAE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ual FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ual OCA], [https://pdbe.org/3ual PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ual RCSB], [https://www.ebi.ac.uk/pdbsum/3ual PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ual 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=3ual FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ual OCA], [https://pdbe.org/3ual PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ual RCSB], [https://www.ebi.ac.uk/pdbsum/3ual PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ual ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/1433E_HUMAN 1433E_HUMAN]] Distal 17p13.3 microdeletion syndrome;17p13.3 microduplication syndrome;Miller-Dieker syndrome. [[https://www.uniprot.org/uniprot/MLF1_HUMAN MLF1_HUMAN]] A chromosomal aberration involving MLF1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with NPM1/NPM.
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[https://www.uniprot.org/uniprot/1433E_HUMAN 1433E_HUMAN] Distal 17p13.3 microdeletion syndrome;17p13.3 microduplication syndrome;Miller-Dieker syndrome.
== Function ==
== Function ==
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[[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/MLF1_HUMAN MLF1_HUMAN]] Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses RFWD2/COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus.<ref>PMID:15861129</ref>
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ual" style="background-color:#fffaf0;"></div>
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==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]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ottmann, C]]
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[[Category: Ottmann C]]
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[[Category: Weyand, M]]
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[[Category: Weyand M]]
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[[Category: Adapter protein]]
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[[Category: All helical]]
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[[Category: Phosphopetide]]
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[[Category: Signaling protein-protein binding complex]]
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Current revision

Crystal Structure of 14-3-3 epsilon with Mlf1 peptide

PDB ID 3ual

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