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| <StructureSection load='5l2q' size='340' side='right'caption='[[5l2q]], [[Resolution|resolution]] 2.53Å' scene=''> | | <StructureSection load='5l2q' size='340' side='right'caption='[[5l2q]], [[Resolution|resolution]] 2.53Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5l2q]] is a 4 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=5L2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L2Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l2q]] is a 4 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=5L2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L2Q FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STK40, SGK495, SHIK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.53Å</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5l2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l2q OCA], [https://pdbe.org/5l2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l2q RCSB], [https://www.ebi.ac.uk/pdbsum/5l2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l2q ProSAT]</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=5l2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l2q OCA], [http://pdbe.org/5l2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l2q RCSB], [http://www.ebi.ac.uk/pdbsum/5l2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l2q ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/STK40_HUMAN STK40_HUMAN]] May be a negative regulator of NF-kappa-B and p53-mediated gene transcription.<ref>PMID:13679039</ref> | + | [https://www.uniprot.org/uniprot/STK40_HUMAN STK40_HUMAN] May be a negative regulator of NF-kappa-B and p53-mediated gene transcription.<ref>PMID:13679039</ref> |
| <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== |
- | *[[Serine/threonine protein kinase|Serine/threonine protein kinase]] | + | *[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Blacklow SC]] |
- | [[Category: Blacklow, S C]] | + | [[Category: Durzynska I]] |
- | [[Category: Durzynska, I]] | + | [[Category: Uljon S]] |
- | [[Category: Uljon, S]] | + | |
- | [[Category: Pseudokinase sink-homologous serine/threonine-protein kinase sugen kinase 495]]
| + | |
- | [[Category: Transferase]]
| + | |
| Structural highlights
Function
STK40_HUMAN May be a negative regulator of NF-kappa-B and p53-mediated gene transcription.[1]
Publication Abstract from PubMed
Serine/threonine kinase 40 (STK40) was originally identified as a distant homolog of Tribbles-family proteins. Despite accumulating data attesting to the importance of STK40 in a variety of different physiologic processes, little is known about its biological activity or mechanism of action. Here, we show that STK40 interacts with Constitutive Photomorphogenic Protein 1 (COP1), relying primarily on a C-terminal sequence analogous to the motif found in Tribbles proteins. In order to further elucidate structure-function relationships in STK40, we determined the crystal structure of the STK40 kinase homology domain at 2.5 A resolution. The structure, together with ATP-binding assay results, show that STK40 is a pseudokinase, in which substitutions of conserved residues within the kinase domain prevent ATP binding. Although the structure of the kinase homology domain diverges from the analogous region of Trib1, the results reported here suggest functional parallels between STK40 and Tribbles-family proteins as COP1 adaptors.
STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1.,Durzynska I, Xu X, Adelmant G, Ficarro SB, Marto JA, Sliz P, Uljon S, Blacklow SC Structure. 2016 Dec 24. pii: S0969-2126(16)30398-7. doi:, 10.1016/j.str.2016.12.008. PMID:28089446[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huang J, Teng L, Liu T, Li L, Chen D, Li F, Xu LG, Zhai Z, Shu HB. Identification of a novel serine/threonine kinase that inhibits TNF-induced NF-kappaB activation and p53-induced transcription. Biochem Biophys Res Commun. 2003 Oct 3;309(4):774-8. PMID:13679039
- ↑ Durzynska I, Xu X, Adelmant G, Ficarro SB, Marto JA, Sliz P, Uljon S, Blacklow SC. STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1. Structure. 2016 Dec 24. pii: S0969-2126(16)30398-7. doi:, 10.1016/j.str.2016.12.008. PMID:28089446 doi:http://dx.doi.org/10.1016/j.str.2016.12.008
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