1ian

From Proteopedia

Revision as of 15:21, 12 November 2007

HUMAN P38 MAP KINASE INHIBITOR COMPLEX

Overview

The crystal structure of human p38 mitogen-activated protein (MAP) kinase, in complex with a potent and highly specific pyridinyl-imidazole inhibitor, has been determined at 2.0 A resolution. The structure of the kinase, which is in its unphosphorylated state, is similar to that of the, closely-related ERK2. The inhibitor molecule is bound in the ATP pocket. A, hydrogen bond is made between the pyridyl nitrogen of the inhibitor and, the main chain amido nitrogen of residue 109, analogous to the interaction, from the N1 atom of ATP. The crystal structure provides possible, explanations for the specificity of this class of inhibitors. Other, protein kinase inhibitors may achieve their specificity through a similar, mechanism. The structure also reveals a possible second binding site for, this inhibitor, with currently unknown function.

About this Structure

1IAN is a Single protein structure of sequence from Homo sapiens with D13 as ligand. Full crystallographic information is available from OCA.

Reference

A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket., Tong L, Pav S, White DM, Rogers S, Crane KM, Cywin CL, Brown ML, Pargellis CA, Nat Struct Biol. 1997 Apr;4(4):311-6. PMID:9095200

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