| Autor: |
Senior MM; Department of Structural Chemistry, Schering-Plough Research Institute, 2015 Galloping Hill Road, Kenilworth, NJ, 07033, U.S.A., Frederick AF, Black S, Murgolo NJ, Perkins LM, Wilson O, Snow ME, Wang YS |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biomolecular NMR [J Biomol NMR] 1998 Feb; Vol. 11 (2), pp. 153-64. |
| DOI: |
10.1023/A:1008250309874 |
| Abstrakt: |
A set of high-resolution three-dimensional solution structures of the Src homology region-2 (SH2) domain of the growth factor receptor-bound protein-2 was determined using heteronuclear NMR spectroscopy. The NMR data used in this study were collected on a stable monomeric protein solution that was free of protein aggregates and proteolysis. The solution structure was determined based upon a total of 1439 constraints, which included 1326 nuclear Overhauser effect distance constraints, 70 hydrogen bond constraints, and 43 dihedral angle constraints. Distance geometry-simulated annealing calculations followed by energy minimization yielded a family of 18 structures that converged to a root-mean-square deviation of 1.09 A for all backbone atoms and 0.40 A for the backbone atoms of the central beta-sheet. The core structure of the SH2 domain contains an antiparallel beta-sheet flanked by two parallel alpha-helices displaying an overall architecture that is similar to other known SH2 domain structures. This family of NMR structures is compared to the X-ray structure and to another family of NMR solution structures determined under different solution conditions. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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