3ggf: Difference between revisions

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{{Seed}}
[[Image:3ggf.png|left|200px]]


<!--
==Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin==
The line below this paragraph, containing "STRUCTURE_3ggf", creates the "Structure Box" on the page.
<StructureSection load='3ggf' size='340' side='right'caption='[[3ggf]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3ggf]] 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=3GGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GGF FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=GVD:[4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)AMINO]QUINAZOLIN-2-YL}IMINO)CYCLOHEXA-2,5-DIEN-1-YL]ACETONITRILE'>GVD</scene></td></tr>
{{STRUCTURE_3ggf|  PDB=3ggf  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ggf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggf OCA], [https://pdbe.org/3ggf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ggf RCSB], [https://www.ebi.ac.uk/pdbsum/3ggf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/STK26_HUMAN STK26_HUMAN] Mediator of cell growth (PubMed:11641781, PubMed:17360971). Modulates apoptosis (PubMed:11641781, PubMed:17360971). In association with STK24 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation (PubMed:27807006).<ref>PMID:11641781</ref> <ref>PMID:17360971</ref> <ref>PMID:27807006</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ggf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: The serine/threonine mammalian Ste-20 like kinases (MSTs) are key regulators of apoptosis, cellular proliferation as well as polarization. Deregulation of MSTs has been associated with disease progression in prostate and colorectal cancer. The four human MSTs are regulated differently by C-terminal regions flanking the catalytic domains. PRINCIPAL FINDINGS: We have determined the crystal structure of kinase domain of MST4 in complex with an ATP-mimetic inhibitor. This is the first structure of an inactive conformation of a member of the MST kinase family. Comparison with active structures of MST3 and MST1 revealed a dimeric association of MST4 suggesting an activation loop exchanged mechanism of MST4 auto-activation. Together with a homology model of MST2 we provide a comparative analysis of the kinase domains for all four members of the human MST family. SIGNIFICANCE: The comparative analysis identified new structural features in the MST ATP binding pocket and has also defined the mechanism for autophosphorylation. Both structural features may be further explored for inhibitors design. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.


===Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin===
Structural comparison of human mammalian ste20-like kinases.,Record CJ, Chaikuad A, Rellos P, Das S, Pike AC, Fedorov O, Marsden BD, Knapp S, Lee WH PLoS One. 2010 Aug 6;5(8):e11905. PMID:20730082<ref>PMID:20730082</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ggf" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20730082}}, adds the Publication Abstract to the page
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20730082 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_20730082}}
__TOC__
 
</StructureSection>
==About this Structure==
3GGF is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGF OCA].
 
==Reference==
<ref group="xtra">PMID:20730082</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C.]]
[[Category: Bountra C]]
[[Category: Chaikuad, A.]]
[[Category: Chaikuad A]]
[[Category: Das, S.]]
[[Category: Das S]]
[[Category: Delft, F Von.]]
[[Category: Edwards AM]]
[[Category: Edwards, A M.]]
[[Category: Eidarus S]]
[[Category: Eidarus, S.]]
[[Category: Fedorov O]]
[[Category: Fedorov, O.]]
[[Category: Filippakopoulos P]]
[[Category: Filippakopoulos, P.]]
[[Category: Knapp S]]
[[Category: Knapp, S.]]
[[Category: Pike ACW]]
[[Category: Pike, A C.W.]]
[[Category: Rellos P]]
[[Category: Rellos, P.]]
[[Category: Roos AK]]
[[Category: Roos, A K.]]
[[Category: Savitsky P]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Sethi R]]
[[Category: Savitsky, P.]]
[[Category: Weigelt J]]
[[Category: Sethi, R.]]
[[Category: Von Delft F]]
[[Category: Weigelt, J.]]
[[Category: Apoptosis]]
[[Category: Atp-binding]]
[[Category: Golgi apparatus]]
[[Category: Kinase]]
[[Category: Magnesium]]
[[Category: Metal-binding]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:15:32 2010''

Latest revision as of 10:05, 6 September 2023

Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolinCrystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin

Structural highlights

3ggf 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 2.35Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STK26_HUMAN Mediator of cell growth (PubMed:11641781, PubMed:17360971). Modulates apoptosis (PubMed:11641781, PubMed:17360971). In association with STK24 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation (PubMed:27807006).[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: The serine/threonine mammalian Ste-20 like kinases (MSTs) are key regulators of apoptosis, cellular proliferation as well as polarization. Deregulation of MSTs has been associated with disease progression in prostate and colorectal cancer. The four human MSTs are regulated differently by C-terminal regions flanking the catalytic domains. PRINCIPAL FINDINGS: We have determined the crystal structure of kinase domain of MST4 in complex with an ATP-mimetic inhibitor. This is the first structure of an inactive conformation of a member of the MST kinase family. Comparison with active structures of MST3 and MST1 revealed a dimeric association of MST4 suggesting an activation loop exchanged mechanism of MST4 auto-activation. Together with a homology model of MST2 we provide a comparative analysis of the kinase domains for all four members of the human MST family. SIGNIFICANCE: The comparative analysis identified new structural features in the MST ATP binding pocket and has also defined the mechanism for autophosphorylation. Both structural features may be further explored for inhibitors design. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.

Structural comparison of human mammalian ste20-like kinases.,Record CJ, Chaikuad A, Rellos P, Das S, Pike AC, Fedorov O, Marsden BD, Knapp S, Lee WH PLoS One. 2010 Aug 6;5(8):e11905. PMID:20730082[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Lin JL, Chen HC, Fang HI, Robinson D, Kung HJ, Shih HM. MST4, a new Ste20-related kinase that mediates cell growth and transformation via modulating ERK pathway. Oncogene. 2001 Oct 4;20(45):6559-69. doi: 10.1038/sj.onc.1204818. PMID:11641781 doi:http://dx.doi.org/10.1038/sj.onc.1204818
  2. ↑ Ma X, Zhao H, Shan J, Long F, Chen Y, Chen Y, Zhang Y, Han X, Ma D. PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway. Mol Biol Cell. 2007 Jun;18(6):1965-78. Epub 2007 Mar 14. PMID:17360971 doi:10.1091/mbc.E06-07-0608
  3. ↑ Mardakheh FK, Self A, Marshall CJ. RHO binding to FAM65A regulates Golgi reorientation during cell migration. J Cell Sci. 2016 Dec 15;129(24):4466-4479. doi: 10.1242/jcs.198614. Epub 2016 Nov, 2. PMID:27807006 doi:http://dx.doi.org/10.1242/jcs.198614
  4. ↑ Record CJ, Chaikuad A, Rellos P, Das S, Pike AC, Fedorov O, Marsden BD, Knapp S, Lee WH. Structural comparison of human mammalian ste20-like kinases. PLoS One. 2010 Aug 6;5(8):e11905. PMID:20730082 doi:10.1371/journal.pone.0011905

3ggf, resolution 2.35Å

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