1BMK

THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB218655

Summary for 1BMK

• Entry DOI: 10.2210/pdb1bmk/pdb
• Descriptor: PROTEIN (MAP KINASE P38), 4-(FLUOROPHENYL)-1-CYCLOPROPYLMETHYL-5-(2-AMINO-4-PYRIMIDINYL)IMIDAZOLE (3 entities in total)
• Functional Keywords: transferase, inhibitors, map kinase, serine/ threonine-protein kinase, p38
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : Q16539
• Total number of polymer chains: 1
• Total formula weight: 43687.65

Authors

Wang, Z.,Canagarajah, B.,Boehm, J.C.,Kassis, S.,Cobb, M.H.,Young, P.R.,Abdel-Meguid, S.,Adams, J.L.,Goldsmith, E.J. (deposition date: 1998-07-23, release date: 1999-07-23, Last modification date: 2024-04-03)

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

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: 9753691
DOI: 10.1016/S0969-2126(98)00113-0

Experimental method

X-RAY DIFFRACTION (2.4 Å)