Abstract
The hematopoietic cellular kinase (Hck) is a member of the Src family of non-receptor protein–tyrosine kinases and participates in signal transduction events regulating the growth, differentiation and function of phagocytes. The secondary structure of the SH2 domain for Hck was determined for a 13C/ 15N-enriched sample using multi-dimensional NMR spectroscopy. The secondary structure for the domain was determined from chemical shift indices [ 1Hα, 13Cα and 13C′], sequential NOEs [ d αN(i, i+1) and d NN(i, i+1)], and 3 J αN scalar coupling constants. The Hck SH2 domain consists of two α-helices and seven β-strands. Complementary strands of β-sheets were identified from long-range NOEs using a novel 3D, 13C/ 15N-edited HMQC-NOESY-(HCACO)NH experiment that correlated 1Hα resonances between β-strands. The secondary structure for Hck SH2 is similar to that predicted from the sequence alignment of the Src-family protein tyrosine kinases.
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