1994
DOI: 10.1111/j.1432-1033.1994.tb20077.x
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Structural Determinants of Substrate Selection by the Human Insulin‐Receptor Protein‐Tyrosine Kinase

Abstract: Using NMR spectroscopy to visualise tyrosine phosphorylation kinetics in real time, we have investigated the sequence‐dependent determinants of the selectivity of the human insulin receptor protein‐tyrosine kinase for different tyrosine residues. The peptides used encompass the multipletyrosine‐containing autophosphorylation site sequences from the insulin receptor kinase core domain (Tyr1158, Tyr162 and Tyr1163) and from its specific C‐terminal tail domain (Tyr1328 and Tyr1334). Comparison of the phosphorylat… Show more

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Cited by 10 publications
(7 citation statements)
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“…Structural information is particularly limited, due in part to the difficulty of obtaining sufficient purified protein in a specific modification state. X-ray crystallography has determined atomic-resolution structures for a few tens of phosphorylated proteins [3], whereas nuclear magnetic resonance (NMR) experiments have elucidated structure and dynamics of a similar number of phosphorylated peptides and small proteins in solution [410]. Electron paramagnetic resonance (EPR) and circular dichroism experiments can also provide information on conformational change due to phosphorylation [11], but do not provide atomic detail.…”
Section: Introductionmentioning
confidence: 99%
“…Structural information is particularly limited, due in part to the difficulty of obtaining sufficient purified protein in a specific modification state. X-ray crystallography has determined atomic-resolution structures for a few tens of phosphorylated proteins [3], whereas nuclear magnetic resonance (NMR) experiments have elucidated structure and dynamics of a similar number of phosphorylated peptides and small proteins in solution [410]. Electron paramagnetic resonance (EPR) and circular dichroism experiments can also provide information on conformational change due to phosphorylation [11], but do not provide atomic detail.…”
Section: Introductionmentioning
confidence: 99%
“…Structural information is particularly limited, due in part to the difficulty of obtaining sufficient purified protein in a specific modification state. X-ray crystallography has determined atomic-resolution structures for a few tens of phosphorylated proteins [3], whereas nuclear magnetic resonance (NMR) experiments have elucidated structure and dynamics of a similar number of phosphorylated peptides and small proteins in solution [4][5][6][7][8][9][10]. Electron paramagnetic resonance (EPR) and circular dichroism experiments can also provide information on conformational change due to phosphorylation [11], but do not provide atomic detail.…”
Section: Introductionmentioning
confidence: 99%
“…A recent mass spectrometry study of 162 cytosolic phosphoproteins provided an experimental confirmation: out of 512 phosphorylation sites, 97% occurred outside of structured domains, and 86% occurred in regions of protein disorder (Collins, et al, 2008). Nonetheless, there are examples of ordered phosphorylation sites (Johnson and Lewis, 2001; Keane, et al, 1994; Quirk, et al, 1996; Tholey, et al, 2001) and a number of structures containing phosphorylated sites have been deposited in PDB (see Data Sets section). In addition, several studies addressed conformational changes in proteins following the addition of the phosphate group (e.g.…”
Section: Experiments and Resultsmentioning
confidence: 99%