Probing the nature of interactions in SH2 binding interfaces--evidence from electrospray ionization mass spectrometry.

Chung, EW; Henriques, DA; Renzoni, D; Morton, CJ; Mulhern, TD; Pitkeathly, MC; Ladbury, JE; Robinson, CV

Abstract:

We have adopted nanoflow electrospray ionization mass spectrometry (ESI-MS) and isothermal titration calorimetry (ITC) to probe the mechanism of peptide recognition by the SH2 domain from the Src family tyrosine kinase protein, Fyn. This domain is involved in the mediation of intracellular signal transduction pathways by interaction with proteins containing phosphorylated tyrosine (Y*) residues. The binding of tyrosyl phosphopeptides can mimic these interactions. Specificity in these interact...

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APA Style

Chung, E. W., Henriques, D. A., Renzoni, D., Morton, C. J., Mulhern, T. D., Pitkeathly, M. C., Ladbury, J. E., & Robinson, C. V. (1999). Probing the nature of interactions in SH2 binding interfaces--evidence from electrospray ionization mass spectrometry. Protein Science : a Publication of the Protein Society, 8(10), 1962–1970.

MLA Style

Chung, E. W., et al. “Probing the Nature of Interactions in SH2 Binding Interfaces--Evidence from Electrospray Ionization Mass Spectrometry.” Protein Science : a Publication of the Protein Society, vol. 8, no. 10, 1999, pp. 1962–70.

Chicago Style

Chung, EW, DA Henriques, D Renzoni, CJ Morton, TD Mulhern, MC Pitkeathly, JE Ladbury, and CV Robinson. 1999. “Probing the Nature of Interactions in SH2 Binding Interfaces--Evidence from Electrospray Ionization Mass Spectrometry.” Protein Science : a Publication of the Protein Society 8 (10): 1962–70.
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