Hematopoietic cell kinase (Hck) is an important signaling enzyme and a potential drug target for HIV infections and Bcr/Abl-chronic myeloid leukemia. The protein shares the same SH4–Unique–SH3–SH2–kinase multi-domain architecture as the other eight members of the Src family of non-receptor tyrosine kinases. These enzymes are often found anchored to the intracellular side of the membrane via lipidation of the SH4 domain and are integral components of signaling cascades localized at the cell surface. Despite the detailed structural information available for the SH3, SH2, and kinase domains of Hck, the intrinsically disordered nature of the SH4 and Unique domains has resulted in a lack of information for this important region of the protein that is responsible for membrane association. Here, we report the 1H, 15N and 13C chemical shifts of the Hck SH4–Unique domains at pH 4.5.
Src family kinase Hck Intrinsically disordered protein
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The authors thank Benjamin Ramirez and Joseph Sachleben for assistance in NMR data collection and Timofey Karginov for assistance with protein production. This work was supported by the National Institutes of Health through grant R01-CA093577 from the National Cancer Institute.
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