Crystallographic and solution studies of an activation loop mutant of the insulin receptor tyrosine kinase: insights into kinase mechanism (Q27629016)

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A J Ablooglu

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M Frankel

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S M Bishop

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R A Kohanski

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S R Hubbard

Journal of Biological Chemistry

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language of work or name

English

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publication date

30 March 2001

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published in

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volume

276

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issue

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page(s)

10049-55

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cites work

Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes

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The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling

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Analysis of insulin-receptor phosphorylation sites in intact cells by two-dimensional phosphopeptide mapping

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Insulin receptor autophosphorylation. II. Determination of autophosphorylation sites by chemical sequence analysis and identification of the juxtamembrane sites

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Phosphorylation activates the insulin receptor tyrosine protein kinase

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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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The function of GRB2 in linking the insulin receptor to Ras signaling pathways

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Crystal structure of the tyrosine kinase domain of the human insulin receptor

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Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog

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Structural analysis of receptor tyrosine kinases

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Conformational changes in the activation loop of the insulin receptor's kinase domain

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Expression, characterization, and crystallization of the catalytic core of the human insulin receptor protein-tyrosine kinase domain

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Cis-autophosphorylation of juxtamembrane tyrosines in the insulin receptor kinase domain

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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AMoRe: an automated package for molecular replacement

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Triosephosphate isomerase catalysis is diffusion controlled. Appendix: Analysis of triose phosphate equilibria in aqueous solution by 31P NMR.

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Rate-determining steps for tyrosine phosphorylation by the kinase domain of v-fps

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Energetic limits of phosphotransfer in the catalytic subunit of cAMP-dependent protein kinase as measured by viscosity experiments

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Three protein kinase structures define a common motif

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2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor

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Partition analysis and concept of net rate constants as tools in enzyme kinetics

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Protein tyrosine kinase structure and function

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Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism

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Three-dimensional structure of the tyrosine kinase c-Src

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The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions

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Crystal structures of c-Src reveal features of its autoinhibitory mechanism

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Crystal structure of the Src family tyrosine kinase Hck

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Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor

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Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

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Autophosphorylation dependent destabilization of the insulin receptor kinase domain: tryptophan-1175 reports changes in the catalytic cleft

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Divalent ion effects and insights into the catalytic mechanism of protein tyrosine kinase Csk

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release_hzn5ndjhencyzph3f2wnulluze

21 January 2018

Identifiers

DOI

10.1074/JBC.M010161200

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/hzn5ndjhencyzph3f2wnulluze