3p1q
From Proteopedia
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==Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 Peptide and stabilizer fusicoccin A== | ==Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 Peptide and stabilizer fusicoccin A== | ||
<StructureSection load='3p1q' size='340' side='right' caption='[[3p1q]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3p1q' size='340' side='right' caption='[[3p1q]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3p1q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3p1q]] 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=3P1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P1Q FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FSC:FUSICOCCIN'>FSC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FSC:FUSICOCCIN'>FSC</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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o98|2o98]], [[3iqv|3iqv]], [[3m50|3m50]], [[3p1n|3p1n]], [[3p1o|3p1o]], [[3p1p|3p1p]], [[3p1r|3p1r]], [[3p1s|3p1s]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o98|2o98]], [[3iqv|3iqv]], [[3m50|3m50]], [[3p1n|3p1n]], [[3p1o|3p1o]], [[3p1p|3p1p]], [[3p1r|3p1r]], [[3p1s|3p1s]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SFN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SFN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <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=3p1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p1q RCSB], [http://www.ebi.ac.uk/pdbsum/3p1q PDBsum]</span></td></tr> | + | <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=3p1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p1q OCA], [http://pdbe.org/3p1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p1q RCSB], [http://www.ebi.ac.uk/pdbsum/3p1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p1q ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/KCNK9_HUMAN KCNK9_HUMAN]] Intellectual deficit, Birk-Barel type. Birk-Barel mental retardation dysmorphism syndrome (BIBAS) [MIM:[http://omim.org/entry/612292 612292]]: A syndrome characterized by mental retardation, hypotonia, hyperactivity, and facial dysmorphism. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:18678320</ref> | ||
== Function == | == Function == | ||
| - | [[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. | + | [[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. [[http://www.uniprot.org/uniprot/KCNK9_HUMAN KCNK9_HUMAN]] pH-dependent, voltage-insensitive, background potassium channel protein.<ref>PMID:11042359</ref> <ref>PMID:11431495</ref> |
==See Also== | ==See Also== | ||
*[[14-3-3 protein|14-3-3 protein]] | *[[14-3-3 protein|14-3-3 protein]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Anders, C]] | [[Category: Anders, C]] | ||
[[Category: Higuchi, Y]] | [[Category: Higuchi, Y]] | ||
Revision as of 02:58, 5 August 2016
Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 Peptide and stabilizer fusicoccin A
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