Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4.
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.
D000595:Amino Acid Sequence; D000818:Animals; D000939:Epitopes / Q000032:analysis*; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000276:immunology; D046911:Macromolecular Substances; D008297:Male; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D013737:Testis / Q000201:enzymology*; D014961:X-Ray Diffraction / Q000379:methods
D000939:Epitopes; D007527:Isoenzymes; D046911:Macromolecular Substances; D007770:L-Lactate Dehydrogenase