2ldx: Difference between revisions

New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2ldx.jpg|left|200px]]<br /><applet load="2ldx" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2ldx, resolution 2.96&Aring;" />
caption="2ldx, resolution 2.96&Aring;" />
'''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, 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.
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 superseeds 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2LDX OCA].  
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.P.]]
[[Category: Griffith, J P.]]
[[Category: Rossmann, M.G.]]
[[Category: Rossmann, M G.]]
[[Category: oxidoreductase(choh(d)-nad(a))]]
[[Category: oxidoreductase(choh(d)-nad(a))]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:41:41 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:04 2008''

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