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==Crystal structure of human serine threonine kinase-10 bound to novel Bosutinib Isoform 1, previously thought to be Bosutinib==
==Crystal structure of human serine threonine kinase-10 bound to novel Bosutinib Isoform 1, previously thought to be Bosutinib==
<StructureSection load='4bc6' size='340' side='right' caption='[[4bc6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='4bc6' size='340' side='right'caption='[[4bc6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4bc6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3zz2 3zz2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BC6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4bc6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3zz2 3zz2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BC6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=XZN:4-[(3,5-DICHLORO-4-METHOXYPHENYL)AMINO]-6-METHOXY-7-[3-(4-METHYLPIPERAZIN-1-YL)PROPOXY]QUINOLINE-3-CARBONITRILE'>XZN</scene></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]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j7t|2j7t]], [[4aot|4aot]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=XZN:4-[(3,5-DICHLORO-4-METHOXYPHENYL)AMINO]-6-METHOXY-7-[3-(4-METHYLPIPERAZIN-1-YL)PROPOXY]QUINOLINE-3-CARBONITRILE'>XZN</scene></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=4bc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bc6 OCA], [https://pdbe.org/4bc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bc6 RCSB], [https://www.ebi.ac.uk/pdbsum/4bc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bc6 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=4bc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bc6 OCA], [http://pdbe.org/4bc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bc6 RCSB], [http://www.ebi.ac.uk/pdbsum/4bc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bc6 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN]] The disease may be caused by mutations affecting the gene represented in this entry.<ref>PMID:16175573</ref>
[https://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN] The disease may be caused by mutations affecting the gene represented in this entry.<ref>PMID:16175573</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN]] Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.<ref>PMID:11903060</ref> <ref>PMID:12639966</ref> <ref>PMID:19255442</ref>
[https://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN] Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.<ref>PMID:11903060</ref> <ref>PMID:12639966</ref> <ref>PMID:19255442</ref>  
 
==See Also==
*[[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: Non-specific serine/threonine protein kinase]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Azeez, K A]]
[[Category: Azeez KA]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Canning, P]]
[[Category: Canning P]]
[[Category: Chaikuad, A]]
[[Category: Chaikuad A]]
[[Category: Delft, F Von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Elkins J]]
[[Category: Elkins, J]]
[[Category: Knapp S]]
[[Category: Knapp, S]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Muniz JRC]]
[[Category: Muniz, J R.C]]
[[Category: Salah E]]
[[Category: Salah, E]]
[[Category: Savitsky P]]
[[Category: Savitsky, P]]
[[Category: Szklarz M]]
[[Category: Szklarz, M]]
[[Category: Vollmar M]]
[[Category: Vollmar, M]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Von Delft F]]
[[Category: Transferase]]

Latest revision as of 14:47, 20 December 2023

Crystal structure of human serine threonine kinase-10 bound to novel Bosutinib Isoform 1, previously thought to be BosutinibCrystal structure of human serine threonine kinase-10 bound to novel Bosutinib Isoform 1, previously thought to be Bosutinib

Structural highlights

4bc6 is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 3zz2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

STK10_HUMAN The disease may be caused by mutations affecting the gene represented in this entry.[1]

Function

STK10_HUMAN Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.[2] [3] [4]

See Also

References

  1. ↑ Bignell G, Smith R, Hunter C, Stephens P, Davies H, Greenman C, Teague J, Butler A, Edkins S, Stevens C, O'Meara S, Parker A, Avis T, Barthorpe S, Brackenbury L, Buck G, Clements J, Cole J, Dicks E, Edwards K, Forbes S, Gorton M, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jones D, Kosmidou V, Laman R, Lugg R, Menzies A, Perry J, Petty R, Raine K, Shepherd R, Small A, Solomon H, Stephens Y, Tofts C, Varian J, Webb A, West S, Widaa S, Yates A, Gillis AJ, Stoop HJ, van Gurp RJ, Oosterhuis JW, Looijenga LH, Futreal PA, Wooster R, Stratton MR. Sequence analysis of the protein kinase gene family in human testicular germ-cell tumors of adolescents and adults. Genes Chromosomes Cancer. 2006 Jan;45(1):42-6. PMID:16175573 doi:http://dx.doi.org/10.1002/gcc.20265
  2. ↑ Tao L, Wadsworth S, Mercer J, Mueller C, Lynn K, Siekierka J, August A. Opposing roles of serine/threonine kinases MEKK1 and LOK in regulating the CD28 responsive element in T-cells. Biochem J. 2002 Apr 1;363(Pt 1):175-82. PMID:11903060
  3. ↑ Walter SA, Cutler RE Jr, Martinez R, Gishizky M, Hill RJ. Stk10, a new member of the polo-like kinase kinase family highly expressed in hematopoietic tissue. J Biol Chem. 2003 May 16;278(20):18221-8. Epub 2003 Mar 13. PMID:12639966 doi:http://dx.doi.org/10.1074/jbc.M212556200
  4. ↑ Belkina NV, Liu Y, Hao JJ, Karasuyama H, Shaw S. LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation. Proc Natl Acad Sci U S A. 2009 Mar 24;106(12):4707-12. doi:, 10.1073/pnas.0805963106. Epub 2009 Mar 2. PMID:19255442 doi:http://dx.doi.org/10.1073/pnas.0805963106

4bc6, resolution 2.20Å

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