6i2y: Difference between revisions

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==Human STK10 bound to Foretinib==
==Human STK10 bound to Foretinib==
<StructureSection load='6i2y' size='340' side='right' caption='[[6i2y]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
<StructureSection load='6i2y' size='340' side='right'caption='[[6i2y]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6i2y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I2Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I2Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[6i2y]] 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=6I2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I2Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=88Z:N-(3-FLUORO-4-{[6-METHOXY-7-(3-MORPHOLIN-4-YLPROPOXY)QUINOLIN-4-YL]OXY}PHENYL)-N-(4-FLUOROPHENYL)CYCLOPROPANE-1,1-DICARBOXAMIDE'>88Z</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]] 2.56&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=88Z:N-(3-FLUORO-4-{[6-METHOXY-7-(3-MORPHOLIN-4-YLPROPOXY)QUINOLIN-4-YL]OXY}PHENYL)-N-(4-FLUOROPHENYL)CYCLOPROPANE-1,1-DICARBOXAMIDE'>88Z</scene></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=6i2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i2y OCA], [http://pdbe.org/6i2y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i2y RCSB], [http://www.ebi.ac.uk/pdbsum/6i2y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i2y 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=6i2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i2y OCA], [https://pdbe.org/6i2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i2y RCSB], [https://www.ebi.ac.uk/pdbsum/6i2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i2y 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: Non-specific serine/threonine protein kinase]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C]]
[[Category: Large Structures]]
[[Category: Berger, B T]]
[[Category: Arrowsmith C]]
[[Category: Bountra, C]]
[[Category: Berger B-T]]
[[Category: Delft, F von]]
[[Category: Bountra C]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Elkins, J M]]
[[Category: Elkins JM]]
[[Category: Knapp, S]]
[[Category: Knapp S]]
[[Category: Oerum, S]]
[[Category: Oerum S]]
[[Category: Sorrell, F J]]
[[Category: Sorrell FJ]]
[[Category: Complex]]
[[Category: Von Delft F]]
[[Category: Foretinib]]
[[Category: Inhibitor]]
[[Category: Kinase]]
[[Category: Lok]]
[[Category: Transferase]]

Latest revision as of 08:19, 21 November 2024

Human STK10 bound to ForetinibHuman STK10 bound to Foretinib

Structural highlights

6i2y is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.56Å
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

6i2y, resolution 2.56Å

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