2ldx
From Proteopedia
(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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- | [[Image:2ldx.jpg|left|200px]]<br /><applet load="2ldx" size=" | + | [[Image:2ldx.jpg|left|200px]]<br /><applet load="2ldx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ldx, resolution 2.96Å" /> | caption="2ldx, resolution 2.96Å" /> | ||
'''CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4'''<br /> | '''CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4'''<br /> | ||
==Overview== | ==Overview== | ||
- | The atomic structure of mouse testicular apolactate dehydrogenase C4 has | + | 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== | ==About this Structure== | ||
- | 2LDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure | + | 2LDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry 1LDX. Active as [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Griffith, J | + | [[Category: Griffith, J P.]] |
- | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
[[Category: oxidoreductase(choh(d)-nad(a))]] | [[Category: oxidoreductase(choh(d)-nad(a))]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:04 2008'' |
Revision as of 16:07, 21 February 2008
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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 supersedes 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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