| Autor: |
Hogrefe, H H, Griffith, J P, Rossmann, M G, Goldberg, E |
| Zdroj: |
Journal of Biological Chemistry; September 1987, Vol. 262 Issue: 27 p13155-13162, 8p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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