4fzf: Difference between revisions
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The | ==Crystal structure of MST4-MO25 complex with DKI== | ||
<StructureSection load='4fzf' size='340' side='right'caption='[[4fzf]], [[Resolution|resolution]] 3.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fzf]] 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=4FZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FZF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.64Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DKI:5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE'>DKI</scene></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=4fzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzf OCA], [https://pdbe.org/4fzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fzf RCSB], [https://www.ebi.ac.uk/pdbsum/4fzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAB39_HUMAN CAB39_HUMAN] Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mammalian STE20-like kinase MST4 regulates multiple cellular aspects such as cell polarity and proliferation. MST4 acts downstream of LKB1/MO25/STRAD complex to induce brush border formation. MO25 directly interacts with MST4 to promote its kinase activity. Here, we report the crystal structure of MST4 in complex with MO25. Association of MO25 rotates the alphaC helix of MST4 toward its catalytic core, stabilizing the alphaC helix in an active position. The kinase domain of MST4 forms a specific homodimer that is required for trans-autophosphorylation. MO25-stimulated activation of MST4 promotes apoptosis in HEK293T cells. Atomic resolution permitted the study of interface mutations capable of disrupting the MST4-MO25 interaction or the kinase-domain-mediated homodimerization. These mutations impaired MST4 kinase activation and function within the cell. Collectively, our study identifies the activation mechanism of MST4 and provides a structural basis for further functional study. | |||
Structure of the MST4 in Complex with MO25 Provides Insights into Its Activation Mechanism.,Shi Z, Jiao S, Zhang Z, Ma M, Zhang Z, Chen C, Wang K, Wang H, Wang W, Zhang L, Zhao Y, Zhou Z Structure. 2013 Feb 19. pii: S0969-2126(13)00014-2. doi:, 10.1016/j.str.2013.01.007. PMID:23434407<ref>PMID:23434407</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4fzf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Shi ZB]] | |||
[[Category: Zhou ZC]] | |||
Latest revision as of 16:54, 8 November 2023
Crystal structure of MST4-MO25 complex with DKICrystal structure of MST4-MO25 complex with DKI
Structural highlights
FunctionCAB39_HUMAN Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1. Publication Abstract from PubMedMammalian STE20-like kinase MST4 regulates multiple cellular aspects such as cell polarity and proliferation. MST4 acts downstream of LKB1/MO25/STRAD complex to induce brush border formation. MO25 directly interacts with MST4 to promote its kinase activity. Here, we report the crystal structure of MST4 in complex with MO25. Association of MO25 rotates the alphaC helix of MST4 toward its catalytic core, stabilizing the alphaC helix in an active position. The kinase domain of MST4 forms a specific homodimer that is required for trans-autophosphorylation. MO25-stimulated activation of MST4 promotes apoptosis in HEK293T cells. Atomic resolution permitted the study of interface mutations capable of disrupting the MST4-MO25 interaction or the kinase-domain-mediated homodimerization. These mutations impaired MST4 kinase activation and function within the cell. Collectively, our study identifies the activation mechanism of MST4 and provides a structural basis for further functional study. Structure of the MST4 in Complex with MO25 Provides Insights into Its Activation Mechanism.,Shi Z, Jiao S, Zhang Z, Ma M, Zhang Z, Chen C, Wang K, Wang H, Wang W, Zhang L, Zhao Y, Zhou Z Structure. 2013 Feb 19. pii: S0969-2126(13)00014-2. doi:, 10.1016/j.str.2013.01.007. PMID:23434407[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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