The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor

• Published in: Molecular and Cellular Biology 1992-04, Vol.12 (4), p.1451-1459
• Main Authors: KLIPPEL, A, ESCOBEDO, J. A, FANTL, W. J, WILLIAMS, L. T
• Format: Article
• Language: English
• Subjects: 3T3 Cells; Analytical, structural and metabolic biochemistry; Animals; binding; Binding Sites; Biological and medical sciences; C-terminus; DNA Mutational Analysis; domains; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; GTPase-Activating Proteins; Mice; mutation; p85 protein; phosphatidylinositol 3-kinase; Phosphatidylinositol 3-Kinases; phosphorylation; Phosphotransferases - chemistry; Phosphotransferases - metabolism; Platelet-Derived Growth Factor - metabolism; platelet-derived growth factor- beta; Protein Conformation; Protein Kinases - metabolism; Protein-Tyrosine Kinases - metabolism; Proteins - metabolism; receptors; Receptors, Platelet-Derived Growth Factor; requirements; Structure-Activity Relationship; Transferases; Type C Phospholipases - metabolism
• ISSN: 0270-7306; 1098-5549
• DOI: 10.1128/MCB.12.4.1451

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