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J Biol Chem. 1989 Aug 5;264(22):13086-92.

C-terminal truncation of p21H preserves crucial kinetic and structural properties.

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1
Max-Planck-Institut für Medizinische Forschung, Abteilung Biophysik, Heidelberg, Federal Republic of Germany.

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.

PMID:
2502546
[Indexed for MEDLINE]
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