2ldx
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(New page: 200px<br /><applet load="2ldx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ldx, resolution 2.96Å" /> '''CHARACTERIZATION OF ...)
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Revision as of 10:34, 21 November 2007
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CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4
Overview
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.
About this Structure
2LDX is a Single protein structure of sequence from Mus musculus. This structure superseeds the now removed PDB entry 1LDX. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from OCA.
Reference
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
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