3HA8
THE COMPLEX STRUCTURE OF THE MAP KINASE P38/Compound 14b
Summary for 3HA8
| Entry DOI | 10.2210/pdb3ha8/pdb |
| Related | 3HA6 |
| Descriptor | Mitogen-activated protein kinase 14, N~2~-{4-[6-(3,4-dihydroquinolin-1(2H)-ylcarbonyl)-1H-benzimidazol-1-yl]-6-ethoxy-1,3,5-triazin-2-yl}-3-(2,2-dimethyl-4H-1,3-benzodioxin-6-yl)-N-methyl-L-alaninamide (3 entities in total) |
| Functional Keywords | transferase, inhibitor, map kinase, serine/ threonine-protein kinase, p38, atp-binding, kinase, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm (By similarity): Q16539 |
| Total number of polymer chains | 1 |
| Total formula weight | 44046.09 |
| Authors | Zhao, B.,Clark, M.A. (deposition date: 2009-05-01, release date: 2009-08-04, Last modification date: 2023-09-06) |
| Primary citation | Clark, M.A.,Acharya, R.A.,Arico-Muendel, C.C.,Belyanskaya, S.L.,Benjamin, D.R.,Carlson, N.R.,Centrella, P.A.,Chiu, C.H.,Creaser, S.P.,Cuozzo, J.W.,Davie, C.P.,Ding, Y.,Franklin, G.J.,Franzen, K.D.,Gefter, M.L.,Hale, S.P.,Hansen, N.J.,Israel, D.I.,Jiang, J.,Kavarana, M.J.,Kelley, M.S.,Kollmann, C.S.,Li, F.,Lind, K.,Mataruse, S.,Medeiros, P.F.,Messer, J.A.,Myers, P.,O'Keefe, H.,Oliff, M.C.,Rise, C.E.,Satz, A.L.,Skinner, S.R.,Svendsen, J.L.,Tang, L.,van Vloten, K.,Wagner, R.W.,Yao, G.,Zhao, B.,Morgan, B.A. Design, synthesis and selection of DNA-encoded small-molecule libraries. Nat.Chem.Biol., 5:647-654, 2009 Cited by PubMed Abstract: Biochemical combinatorial techniques such as phage display, RNA display and oligonucleotide aptamers have proven to be reliable methods for generation of ligands to protein targets. Adapting these techniques to small synthetic molecules has been a long-sought goal. We report the synthesis and interrogation of an 800-million-member DNA-encoded library in which small molecules are covalently attached to an encoding oligonucleotide. The library was assembled by a combination of chemical and enzymatic synthesis, and interrogated by affinity selection. We describe methods for the selection and deconvolution of the chemical display library, and the discovery of inhibitors for two enzymes: Aurora A kinase and p38 MAP kinase. PubMed: 19648931DOI: 10.1038/nchembio.211 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.48 Å) |
Structure validation
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