Conformational effects of the substitution of ARG for GLY 13 in the ras oncogene-encoded P21 protein

Paul W. Brandt-Rauf, Robert P. Carty, John Carucci, Matthew Avitable, Jack Lubowsky, Matthew R. Pincus

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The effect of the substitution of Arg for Gly 13 on the structure of the transforming region decapeptide (Leu 6-Gly 15) of the ras oncogene encoded P21 protein has been investigated using conformational energy analysis. A human malignancy has been identified that contains a ras gene with a single mutation in the thirteenth codon such that the encoded protein would have Arg substituted for Gly at this position, and transfection of cells in culture with this gene results in malignant transformation. Conformational analysis demonstrates that the Arg 13 decapeptide adopts a conformation identical to that for other peptides with substitutions at position 13 (Asp 13, Val 13) from transforming proteins that is distinctively different from that for peptides (Gly 13, Ser 13) from normal, nontransforming proteins. This is found to be an indirect effect resulting from changes in the conformation of Gly 12 produced by substitutions at position 13. These results are consistent with recent analysis of crystallographic data of proteins on conformational preferences for glycine in tripeptide sequences.

Original languageEnglish
Pages (from-to)349-354
Number of pages6
JournalJournal of Protein Chemistry
Volume7
Issue number4
DOIs
StatePublished - Aug 1988
Externally publishedYes

Keywords

  • P21 protein
  • amino acid substitution
  • conformational energy
  • position 13
  • transformation

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