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Structure paper

TitleBenzothiophene inhibitors of MK2. Part 2: improvements in kinase selectivity and cell potency.
Journal, issue, pagesBioorg. Med. Chem. Lett., Vol. 19, Page 4882-4884, Year 2009
Publish dateJan 22, 2009 (structure data deposition date)
AuthorsAnderson, D.R. / Meyers, M.J. / Kurumbail, R.G. / Caspers, N. / Poda, G.I. / Long, S.A. / Pierce, B.S. / Mahoney, M.W. / Mourey, R.J. / Parikh, M.D.
External linksBioorg. Med. Chem. Lett. / PubMed:19616942
MethodsX-ray diffraction
Resolution1.9 - 3.8 Å
Structure data

PDB-3fyj:
Crystal structure of an optimzied benzothiophene inhibitor bound to MAPKAP Kinase-2 (MK-2)
Method: X-RAY DIFFRACTION / Resolution: 3.8 Å

PDB-3fyk:
Crystal structure of a benzthiophene lead bound to MAPKAP Kinase-2 (MK-2)
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

PDB-3fz1:
Crystal structure of a benzthiophene inhibitor bound to human Cyclin-dependent Kinase-2 (CDK-2)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-B97:
(10R)-10-methyl-3-(6-methylpyridin-3-yl)-9,10,11,12-tetrahydro-8H-[1,4]diazepino[5',6':4,5]thieno[3,2-f]quinolin-8-one

ChemComp-B98:
(3R)-3-(aminomethyl)-9-methoxy-1,2,3,4-tetrahydro-5H-[1]benzothieno[3,2-e][1,4]diazepin-5-one

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / MK-2 / MK2 / MAPKAP-2 / Ser/Thr kinase / MAP kinase / Alternative splicing / ATP-binding / Kinase / Nucleotide-binding / Phosphoprotein / Polymorphism / Serine/threonine-protein kinase / CDK-2 / MAPKAP kinase-2 / cell divison kinase-2 / cyclin / benzothiophene / Cell cycle / Cell division / Mitosis

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