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Journal Article

C−terminal truncation of p21H preserves crucial kinetic and structural properties

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons127936

John,  Jiss
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95189

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95056

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95966

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

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Citation

John, J., Schlichting, I., Schiltz, E., Rösch, P., & Wittinghofer, A. (1989). C−terminal truncation of p21H preserves crucial kinetic and structural properties. Journal of Biological Chemistry, 264(22), 13086-13092. Retrieved from http://www.jbc.org/cgi/content/abstract/264/22/13086.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-AD9D-A
Abstract
The human c−Ha−ras protooncogene product p21C was truncated at the C terminus by 23 amino acids. The resulting G−binding domain, p21 (1−166) = p21C', can be crystallized as a complex with the slowly hydrolyzing GTP analogues guanosin−5'−[beta,gamma−imido]triphosphate, guanosin−5'− [beta,gamma−methylene]triphosphate, and guanosin−5'−O−(3− thiotriphosphate). We show here that this protein has biochemical properties very similar to those of the intact protein. Activating mutations in position 12 (Gly12−−−−Val; Gly12−−−−Arg) have the same effect on the properties of the truncated protein as on intact protein. Nuclear magnetic resonance (NMR) measurements show no apparent effect of the C−terminal deletion on the solution structure of p21. This suggests that neither the structure of the G−binding domain nor any of its biochemical properties are markedly influenced by the truncation