O'Connor Casey, Kovrigin Evgenii L
Biochemistry Department, Medical College of Wisconsin, 8701 Watertown Plank Rd, Milwaukee, WI 53226, USA.
Biomol NMR Assign. 2012 Apr;6(1):91-3. doi: 10.1007/s12104-011-9332-3. Epub 2011 Aug 4.
The small GTPase Ras is an important signaling molecule acting as a molecular switch in eukaryotic cells. Recent findings of global conformational exchange and a putative allosteric binding site in the G domain of Ras opened an avenue to understanding novel aspects of Ras function. To facilitate detailed NMR studies of Ras in physiological solution conditions, we performed backbone resonance assignments of Ras bound to slowly hydrolysable GTP mimic, guanosine 5'-[ß, γ-imido]triphosphate at pH 7.2. Out of 163 non-proline residues of the G domain, signals from backbone amide proton, nitrogen and carbon spins of 127 residues were confidently assigned with the remaining unassigned residues mostly located at the exchange-broadened effectors interface.
小GTP酶Ras是一种重要的信号分子，在真核细胞中充当分子开关。最近关于Ras的G结构域中全局构象交换和一个假定的变构结合位点的发现，为理解Ras功能的新方面开辟了一条途径。为了便于在生理溶液条件下对Ras进行详细的核磁共振研究，我们在pH 7.2时对与缓慢水解的GTP类似物鸟苷5'-[β,γ-亚氨基]三磷酸结合的Ras进行了主链共振归属。在G结构域的163个非脯氨酸残基中，127个残基的主链酰胺质子、氮和碳自旋信号被可靠地归属，其余未归属的残基大多位于交换加宽的效应器界面处。
