1dm2

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[[Image:1dm2.gif|left|200px]]
[[Image:1dm2.gif|left|200px]]
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{{Structure
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|PDB= 1dm2 |SIZE=350|CAPTION= <scene name='initialview01'>1dm2</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1dm2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HMD:4-(5-AMINO-4-OXO-4H-PYRAZOL-3-YL)-2-BROMO-4,5,6,7-TETRAHYDRO-3AH-PYRROLO[2,3-C]AZEPIN-8-ONE'>HMD</scene>
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{{STRUCTURE_1dm2| PDB=1dm2 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm2 OCA], [http://www.ebi.ac.uk/pdbsum/1dm2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dm2 RCSB]</span>
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'''HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR HYMENIALDISINE'''
'''HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR HYMENIALDISINE'''
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[[Category: Kim, S H.]]
[[Category: Kim, S H.]]
[[Category: Thunnissen, A M.]]
[[Category: Thunnissen, A M.]]
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[[Category: cell cycle]]
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[[Category: Cell cycle]]
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[[Category: cell division]]
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[[Category: Cell division]]
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[[Category: inhibition]]
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[[Category: Inhibition]]
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[[Category: mitosis]]
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[[Category: Mitosis]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: protein kinase]]
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[[Category: Protein kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:00:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:44:13 2008''
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Revision as of 11:00, 2 May 2008

Image:1dm2.gif

Template:STRUCTURE 1dm2

HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR HYMENIALDISINE


Overview

BACKGROUND: Over 2000 protein kinases regulate cellular functions. Screening for inhibitors of some of these kinases has already yielded some potent and selective compounds with promising potential for the treatment of human diseases. RESULTS: The marine sponge constituent hymenialdisine is a potent inhibitor of cyclin-dependent kinases, glycogen synthase kinase-3beta and casein kinase 1. Hymenialdisine competes with ATP for binding to these kinases. A CDK2-hymenialdisine complex crystal structure shows that three hydrogen bonds link hymenialdisine to the Glu81 and Leu83 residues of CDK2, as observed with other inhibitors. Hymenialdisine inhibits CDK5/p35 in vivo as demonstrated by the lack of phosphorylation/down-regulation of Pak1 kinase in E18 rat cortical neurons, and also inhibits GSK-3 in vivo as shown by the inhibition of MAP-1B phosphorylation. Hymenialdisine also blocks the in vivo phosphorylation of the microtubule-binding protein tau at sites that are hyperphosphorylated by GSK-3 and CDK5/p35 in Alzheimer's disease (cross-reacting with Alzheimer's-specific AT100 antibodies). CONCLUSIONS: The natural product hymenialdisine is a new kinase inhibitor with promising potential applications for treating neurodegenerative disorders.

About this Structure

1DM2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Inhibition of cyclin-dependent kinases, GSK-3beta and CK1 by hymenialdisine, a marine sponge constituent., Meijer L, Thunnissen AM, White AW, Garnier M, Nikolic M, Tsai LH, Walter J, Cleverley KE, Salinas PC, Wu YZ, Biernat J, Mandelkow EM, Kim SH, Pettit GR, Chem Biol. 2000 Jan;7(1):51-63. PMID:10662688 Page seeded by OCA on Fri May 2 14:00:28 2008

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