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Structural Features that Specify Tyrosine Kinase Activity Deduced from Homology Modeling of the Epidermal Growth Factor Receptor
Daniel R. Knighton, Deborah L. Cadena, Jianhua Zheng, Lynn F. Ten Eyck, Susan S. Taylor, Janusz M. Sowadski and Gordon N. Gill
Proceedings of the National Academy of Sciences of the United States of America
Vol. 90, No. 11 (Jun. 1, 1993), pp. 5001-5005
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2362209
Page Count: 5
You can always find the topics here!Topics: Amino acids, Phosphates, Active sites, Catalysis, Oxygen, Hydrogen bonds, Protons, Phosphorylation, Growth factor receptors, Coordinate systems
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To identify structural features that distinguish protein-tyrosine kinases from protein-serine kinases, a molecular model of the kinase domain of epidermal growth factor receptor was constructed by substituting its amino acid sequence for the amino acid sequence of the catalytic subunit of cAMP-dependent protein kinase in a 2.7-Å refined crystallographic model. General folding was conserved as was the configuration of invariant residues at the active site. Two sequence motifs that distinguish the two families correspond to loops that converge at the active site of the enzyme. A conserved arginine in the catalytic loop is proposed to interact with the γ phosphate of ATP. The second loop provides a binding surface that positions the tyrosine of the substrate. A positively charged surface provides additional sites for substrate recognition.
Proceedings of the National Academy of Sciences of the United States of America © 1993 National Academy of Sciences