Proto-oncogene serine/threonine-protein kinase

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{{STRUCTURE_3cy2| PDB=3cy2 | SIZE=350| SCENE= |right|CAPTION=Pim-1 (grey) complex with consensus peptide (green), inhibitor and Cl- ion [[3cy2]] }}
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<StructureSection load='3cy2' size='350' side='right' scene='' caption='Pim-1 (grey) complex with consensus peptide (green), inhibitor and Cl- ion [[3cy2]]'>
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== Function ==
== Function ==
'''Proto-oncogene serine/threonine-protein kinase (Pim1)''' is the provirus integration site for Moloney murine leukemia virus 1<ref>PMID:15694833</ref>. Pim1 is involved in cell cycle progression, apoptosis, transcriptional activation and signaling pathways. Pim1 phosphorylates and inhibits proapoptotic proteins. For details see [[Student Project 6 for UMass Chemistry 423 Spring 2015]].
'''Proto-oncogene serine/threonine-protein kinase (Pim1)''' is the provirus integration site for Moloney murine leukemia virus 1<ref>PMID:15694833</ref>. Pim1 is involved in cell cycle progression, apoptosis, transcriptional activation and signaling pathways. Pim1 phosphorylates and inhibits proapoptotic proteins. For details see [[Student Project 6 for UMass Chemistry 423 Spring 2015]].
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== Structural highlights ==
== Structural highlights ==
Pim1 is phosphorylated on serine 261 (PSer). The consensus peptide (pimtide) ARKRRRHPSGPPTA binds strongly to Pim1<ref>PMID:22136433</ref>.
Pim1 is phosphorylated on serine 261 (PSer). The consensus peptide (pimtide) ARKRRRHPSGPPTA binds strongly to Pim1<ref>PMID:22136433</ref>.
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</StructureSection>
== 3D Structures of pim-1 ==
== 3D Structures of pim-1 ==

Revision as of 07:59, 28 July 2016

Pim-1 (grey) complex with consensus peptide (green), inhibitor and Cl- ion 3cy2

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3D Structures of pim-1

Updated on 28-July-2016

References

  1. Bachmann M, Moroy T. The serine/threonine kinase Pim-1. Int J Biochem Cell Biol. 2005 Apr;37(4):726-30. PMID:15694833 doi:http://dx.doi.org/10.1016/j.biocel.2004.11.005
  2. Brault L, Menter T, Obermann EC, Knapp S, Thommen S, Schwaller J, Tzankov A. PIM kinases are progression markers and emerging therapeutic targets in diffuse large B-cell lymphoma. Br J Cancer. 2012 Jul 24;107(3):491-500. doi: 10.1038/bjc.2012.272. Epub 2012 Jun, 21. PMID:22722314 doi:http://dx.doi.org/10.1038/bjc.2012.272
  3. Weirauch U, Beckmann N, Thomas M, Grunweller A, Huber K, Bracher F, Hartmann RK, Aigner A. Functional role and therapeutic potential of the pim-1 kinase in colon carcinoma. Neoplasia. 2013 Jul;15(7):783-94. PMID:23814490
  4. Huber K, Brault L, Fedorov O, Gasser C, Filippakopoulos P, Bullock AN, Fabbro D, Trappe J, Schwaller J, Knapp S, Bracher F. 7,8-Dichloro-1-oxo-beta-carbolines as a Versatile Scaffold for the Development of Potent and Selective Kinase Inhibitors with Unusual Binding Modes. J Med Chem. 2012 Jan 12;55(1):403-13. Epub 2012 Jan 3. PMID:22136433 doi:10.1021/jm201286z

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