4ERK
THE COMPLEX STRUCTURE OF THE MAP KINASE ERK2/OLOMOUCINE
Summary for 4ERK
| Entry DOI | 10.2210/pdb4erk/pdb |
| Descriptor | EXTRACELLULAR REGULATED KINASE 2, SULFATE ION, OLOMOUCINE, ... (4 entities in total) |
| Functional Keywords | transferase, serine/threonine-protein kinase, map kinase, erk2 |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 42553.84 |
| Authors | Wang, Z.,Canagarajah, B.,Boehm, J.C.,Cobb, M.H.,Young, P.R.,Abdel-Meguid, S.,Adams, J.L.,Goldsmith, E.J. (deposition date: 1998-07-09, release date: 1999-07-22, Last modification date: 2024-05-22) |
| Primary citation | Wang, Z.,Canagarajah, B.J.,Boehm, J.C.,Kassisa, S.,Cobb, M.H.,Young, P.R.,Abdel-Meguid, S.,Adams, J.L.,Goldsmith, E.J. Structural basis of inhibitor selectivity in MAP kinases. Structure, 6:1117-1128, 1998 Cited by PubMed Abstract: The mitogen-activated protein (MAP) kinases are important signaling molecules that participate in diverse cellular events and are potential targets for intervention in inflammation, cancer, and other diseases. The MAP kinase p38 is responsive to environmental stresses and is involved in the production of cytokines during inflammation. In contrast, the activation of the MAP kinase ERK2 (extracellular-signal-regulated kinase 2) leads to cellular differentiation or proliferation. The anti-inflammatory agent pyridinylimidazole and its analogs (SB [SmithKline Beecham] compounds) are highly potent and selective inhibitors of p38, but not of the closely-related ERK2, or other serine/threonine kinases. Although these compounds are known to bind to the ATP-binding site, the origin of the inhibitory specificity toward p38 is not clear. PubMed: 9753691DOI: 10.1016/S0969-2126(98)00113-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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