Intraresidue 1H-15N-13C' and 1H alpha-13C alpha-13C' dipole-CSA relaxation interference as a source of constraints for structural refinement of metal-binding sites in zinc-finger proteins

Autor:	K, Kloiber, W, Schüler, R, Konrat
Rok vydání:	2001
Předmět:	Models Molecular Carbon Isotopes Binding Sites Magnetic Resonance Spectroscopy Nitrogen Isotopes Protein Conformation Zinc Fingers Models Theoretical Hydrogen Protein Binding
Zdroj:	Journal of biomolecular NMR. 19(4)
ISSN:	0925-2738
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::9dc6a23af1cf846b9b9c9d37ea4bf916 https://pubmed.ncbi.nlm.nih.gov/11370780 Zobrazit plný text záznamu Full text from SpringerLink