Kloiber K, Schüler W, Konrat R
Institute of Organic Chemistry, University of Innsbruck, Austria.
J Biomol NMR. 2001 Apr;19(4):347-54. doi: 10.1023/a:1011248220839.
1H(i)-15 N(i)-13C'(i) dipole-chemical shift anisotropy (CSA) relaxation interference was quantified for the 13C,15N labeled zinc-finger protein qCRP2(LIM2). The cross-correlation rates obtained for residues located in the metal coordination sites of qCRP2(LIM2) show a high degree of correlation with the peptide plane torsion angles phi and psi taken from the solution structure. 1H(i)-15N(i)-13C'(i) as well as 13C alpha(i)-1H alpha(i)-13C'(i) dipole-CSA cross-correlation rates were subsequently used to improve the geometry of the metal binding site. The optimized dihedral angles of the two zinc-binding sites in qCRP2(LIM2) are in better agreement with values obtained from crystal structures of other zinc-finger proteins and thus establish the utility of this approach to improve the metal-binding site geometry of zinc-finger proteins studied by NMR spectroscopy in solution.
对13C、15N标记的锌指蛋白qCRP2（LIM2）的1H(i)-15N(i)-13C'(i)偶极-化学位移各向异性（CSA）弛豫干扰进行了定量分析。在qCRP2（LIM2）的金属配位位点中获得的位于残基处的交叉相关速率与从溶液结构中获取的肽平面扭转角phi和psi显示出高度相关性。随后，利用1H(i)-15N(i)-13C'(i)以及13Cα(i)-1Hα(i)-13C'(i)偶极-CSA交叉相关速率来优化金属结合位点的几何结构。qCRP2（LIM2）中两个锌结合位点的优化二面角与从其他锌指蛋白晶体结构中获得的值更相符，从而确立了这种方法在改善通过溶液核磁共振光谱研究的锌指蛋白金属结合位点几何结构方面的实用性。
