ISSN:
1573-5001
Keywords:
Grb2
;
SH2 domain
;
Heteronuclear NMR
;
CSI method
;
Chemical shift assignments
;
Secondary structure
;
Isotopic enrichment
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary 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 15N-enriched amino acids. Using the Chemical Shift Index (CSI) method, the chemical shift indices of four nuclei, 1Hα, 13Cα, 13Cβ and 13CO, 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 β-sheet and two α-helices. In general, the secondary structural elements determined from the CSI method agree well with those predicted from the sequence alignment.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00203819
Permalink
