2LDX

CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4

Replaces:  1LDX

Summary for 2LDX

• Entry DOI: 10.2210/pdb2ldx/pdb
• Descriptor: APO-LACTATE DEHYDROGENASE (2 entities in total)
• Functional Keywords: oxidoreductase(choh(d)-nad(a))
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: P00342
• Total number of polymer chains: 4
• Total formula weight: 143466.42

Authors

Griffith, J.P.,Rossmann, M.G. (deposition date: 1987-11-25, release date: 1989-04-19, Last modification date: 2023-09-06)

Primary citation

Hogrefe, H.H.,Griffith, J.P.,Rossmann, M.G.,Goldberg, E.
Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4.
J.Biol.Chem., 262:13155-13162, 1987

PubMed 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.

PubMed: 2443489

Experimental method

X-RAY DIFFRACTION (2.96 Å)