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

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.

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Genre: Journal Article
Alternative Title : C−terminal truncation of p21H preserves crucial kinetic and structural properties

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 Creators:
John, Jiss1, 2, Author           
Schlichting, Ilme3, 4, Author           
Schiltz, Emile, Author
Rösch, Paul4, Author           
Wittinghofer, Alfred4, Author           
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497741              
3Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society, ou_1856341              
4Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 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

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Language(s): eng - English
 Dates: 1989-02-281989-08-05
 Publication Status: Issued
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 Rev. Type: Peer
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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 264 (22) Sequence Number: - Start / End Page: 13086 - 13092 Identifier: -