3smo

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==Crystal structure of human 14-3-3 sigma C38V/N166H in complex with TASK-3 peptide and stabilizer Fusicoccin J aglycone==
==Crystal structure of human 14-3-3 sigma C38V/N166H in complex with TASK-3 peptide and stabilizer Fusicoccin J aglycone==
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<StructureSection load='3smo' size='340' side='right' caption='[[3smo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='3smo' size='340' side='right'caption='[[3smo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3smo]] is a 2 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=3SMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SMO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3smo]] 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=3SMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SMO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FJA:FUSICOCCIN+J+AGLYCONE'>FJA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=FJA:FUSICOCCIN+J+AGLYCONE'>FJA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<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>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o98|2o98]], [[3lw1|3lw1]], [[3iqu|3iqu]]</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;'>[[2o98|2o98]], [[3lw1|3lw1]], [[3iqu|3iqu]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HME1, SFN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HME1, SFN ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3smo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3smo OCA], [http://pdbe.org/3smo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3smo RCSB], [http://www.ebi.ac.uk/pdbsum/3smo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3smo ProSAT]</span></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=3smo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3smo OCA], [https://pdbe.org/3smo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3smo RCSB], [https://www.ebi.ac.uk/pdbsum/3smo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3smo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/1433S_HUMAN 1433S_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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.
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[[https://www.uniprot.org/uniprot/1433S_HUMAN 1433S_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. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[14-3-3 protein|14-3-3 protein]]
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*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Anders, C]]
[[Category: Anders, C]]
[[Category: Ottmann, C]]
[[Category: Ottmann, C]]

Revision as of 08:55, 5 May 2021

Crystal structure of human 14-3-3 sigma C38V/N166H in complex with TASK-3 peptide and stabilizer Fusicoccin J aglycone

PDB ID 3smo

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