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Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronuclear NMR spectroscopy

✍ Scribed by Yu-Sen Wang; Anne F. Frederick; Mary M. Senior; Barbara A. Lyons; Stuart Black; Paul Kirschmeier; Louise M. Perkins; Oswald Wilson

Publisher
Springer Netherlands
Year
1996
Tongue
English
Weight
832 KB
Volume
7
Category
Article
ISSN
0925-2738

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✦ Synopsis

The growth factor receptor-bound protein-2 (Grb2) is an adaptor protein that mediates signal transduction pathways. Chemical shift assignments were obtained for the SH2 domain of Grb2 by heteronuclear NMR spectroscopy, employing the uniformly 13C-/15N-enriched protein as well as the protein containing selectively lSN-enriched amino acids. Using the Chemical Shift Index (CSI) method, the chemical shift indices of four nuclei, IH ~, J3C~, 13C~ and ~3CO, were used to derive the secondary structure of the protein. Nuclear Overhauser enhancements (NOEs) were then employed to confirm the secondary structure. The CSI results were compared to the secondary structural elements predicted for the Grb2 SH2 domain from a sequence alignment [Lee et al. (1994) Structure, 2, 423-438]. The core structure of the SH2 domain contains an antiparallel [3-sheet and two c~-helices. In general, the secondary structural elements determined from the CSI method agree well with those predicted from the sequence alignment.

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