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1BMK

THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB218655

Summary for 1BMK
Entry DOI10.2210/pdb1bmk/pdb
DescriptorPROTEIN (MAP KINASE P38), 4-(FLUOROPHENYL)-1-CYCLOPROPYLMETHYL-5-(2-AMINO-4-PYRIMIDINYL)IMIDAZOLE (3 entities in total)
Functional Keywordstransferase, inhibitors, map kinase, serine/ threonine-protein kinase, p38
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm : Q16539
Total number of polymer chains1
Total formula weight43687.65
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 citationWang, 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: 9753691
DOI: 10.1016/S0969-2126(98)00113-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

226707

数据于2024-10-30公开中

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