title: The three-dimensional solution structure of the SRC homology domain-2 of the growth factor receptor-bound protein-2.
abstract: 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.
authors.affiliation: Department of Structural Chemistry, Schering-Plough Research Institute, 2015 Galloping Hill Road, Kenilworth, NJ, 07033, U.S.A.
authors.forename: M M
authors.initials: MM
authors.lastname: Senior
authors.forename: A F
authors.initials: AF
authors.lastname: Frederick
authors.forename: S
authors.initials: S
authors.lastname: Black
authors.forename: N J
authors.initials: NJ
authors.lastname: Murgolo
authors.forename: L M
authors.initials: LM
authors.lastname: Perkins
authors.forename: O
authors.initials: O
authors.lastname: Wilson
authors.forename: M E
authors.initials: ME
authors.lastname: Snow
authors.forename: Y S
authors.initials: YS
authors.lastname: Wang