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Protein farnesyltransferase.

Publication ,  Journal Article
Park, HW; Beese, LS
Published in: Curr Opin Struct Biol
December 1997

In the past year, the crystal structure of alpha beta heterodimeric protein farnesyltransferase from rat was reported to a resolution of 2.25 A. Farnesyltransferase catalyzes the essential post-translational lipidation of Ras and several other cellular signal transduction proteins. The structure provides a foundation for understanding the specificity and mechanism of protein prenylation and may aid in the design of new anticancer therapeutics.

Duke Scholars

Published In

Curr Opin Struct Biol

DOI

ISSN

0959-440X

Publication Date

December 1997

Volume

7

Issue

6

Start / End Page

873 / 880

Location

England

Related Subject Headings

  • ras Proteins
  • Zinc
  • Substrate Specificity
  • Rats
  • Protein Structure, Secondary
  • Protein Prenylation
  • Mutagenesis, Site-Directed
  • Molecular Sequence Data
  • Models, Molecular
  • Dimerization
 

Citation

APA
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MLA
NLM
Park, H. W., & Beese, L. S. (1997). Protein farnesyltransferase. Curr Opin Struct Biol, 7(6), 873–880. https://doi.org/10.1016/s0959-440x(97)80160-1
Park, H. W., and L. S. Beese. “Protein farnesyltransferase.Curr Opin Struct Biol 7, no. 6 (December 1997): 873–80. https://doi.org/10.1016/s0959-440x(97)80160-1.
Park HW, Beese LS. Protein farnesyltransferase. Curr Opin Struct Biol. 1997 Dec;7(6):873–80.
Park, H. W., and L. S. Beese. “Protein farnesyltransferase.Curr Opin Struct Biol, vol. 7, no. 6, Dec. 1997, pp. 873–80. Pubmed, doi:10.1016/s0959-440x(97)80160-1.
Park HW, Beese LS. Protein farnesyltransferase. Curr Opin Struct Biol. 1997 Dec;7(6):873–880.
Journal cover image

Published In

Curr Opin Struct Biol

DOI

ISSN

0959-440X

Publication Date

December 1997

Volume

7

Issue

6

Start / End Page

873 / 880

Location

England

Related Subject Headings

  • ras Proteins
  • Zinc
  • Substrate Specificity
  • Rats
  • Protein Structure, Secondary
  • Protein Prenylation
  • Mutagenesis, Site-Directed
  • Molecular Sequence Data
  • Models, Molecular
  • Dimerization