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Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase
Author(s) -
Zhang Weixing,
Smithgall Thomas E.,
Gmeiner William H.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00255-x
Subject(s) - proto oncogene tyrosine protein kinase src , sh2 domain , protein secondary structure , chemistry , signal transduction , nuclear magnetic resonance spectroscopy , tyrosine protein kinase csk , kinase , sh3 domain , tyrosine kinase , circular dichroism , stereochemistry , crystallography , biochemistry
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 13 C/ 15 N‐enriched sample using multi‐dimensional NMR spectroscopy. The secondary structure for the domain was determined from chemical shift indices [ 1 Hα, 13 Cα and 13 C′], 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, 13 C/ 15 N‐edited HMQC‐NOESY‐(HCACO)NH experiment that correlated 1 Hα 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.