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NMR studies of protein-nucleotide interactions: p21 and adenylate kinase

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Schlichting,  Ilme
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Rösch,  Paul
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Vetter, I. R., Schlichting, I., Wittinghofer, A., Goody, R. S., & Rösch, P. (1989). NMR studies of protein-nucleotide interactions: p21 and adenylate kinase. Bulletin of Magnetic Resonance, 11(3-4), 203-209.


Cite as: https://hdl.handle.net/21.11116/0000-000B-6EA6-F
Abstract
We performed one- and two-dimensional nuclear magnetic resonance (NMR) studies, in particular substrate-protein nuclear Overhauser effect (NOESY) measurements, as well as nucleotide and P ,P -bis(5'-adenosine)-pentaphosphate (APcA) titrations of the E. coli adenylate kinase. Also, the same types of experiment were performed with the H-ras oncogene product p21. These experiments led us to the following conclusions:


1. AP5A'Mg2+ binds to both nucleotide sites simultaneously and thus simulates the active complex.


2. The ATP-Mgz adenine in the AKEC.-AP5A-Mgz+ complex is located close to His134 and Phe , i. e the ATP'Mgz site in solution is identical to the ATP'Mgz+ site in the crystal (Muller, C. W. , & Schulz, G. E. (1988) J. Mol. Biol. 202, 909-912).


3. The AKE C 'G-loop' with bound ATP'Mg is structurally highly homologous to the loop region in the oncogene product p21 with bound GTP'Mg in solution as well as in the crystal (Pai, E. F. , Kabsch with bound GTP'Mg in solution as well as in the crystal (Pai, E. F. , Kabsch, W. , John, J., Holmes, K. C. , & Wittinghofer, A. (1989) Nature, in press).