Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4.

H. H. Hogrefe*, J. P. Griffith, M. G. Rossmann, E. Goldberg

*Corresponding author for this work

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

The atomic structure of mouse testicular apolactate dehydrogenase C4 has been refined to 3.0-A resolution yielding a final crystallographic R-factor of 0.256. Comparison with the refined structure of dogfish apolactate dehydrogenase A4 shows that equivalent secondary structure elements are essentially in the same position relative to the molecular 2-fold axes, except for the helices alpha D, alpha E, and alpha 2G in the vicinity of the active center, and the carboxyl-terminal helix alpha H. The positions of antigenic peptides correlate best with surface accessibilities of the monomer rather than of the full tetrameric molecule.

Original languageEnglish (US)
Pages (from-to)13155-13162
Number of pages8
JournalThe Journal of biological chemistry
Volume262
Issue number27
StatePublished - Sep 25 1987

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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