Structural highlights
Function
[LDHC_MOUSE] Possible role in sperm motility (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4.,Hogrefe HH, Griffith JP, Rossmann MG, Goldberg E J Biol Chem. 1987 Sep 25;262(27):13155-62. PMID:2443489[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hogrefe HH, Griffith JP, Rossmann MG, Goldberg E. Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4. J Biol Chem. 1987 Sep 25;262(27):13155-62. PMID:2443489
