2ldx: Difference between revisions

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~~'''~~CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4~~'''~~

===CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4===

~~==Overview==~~

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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 line below this paragraph, {{ABSTRACT_PUBMED_2443489}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 2443489 is the PubMed ID number.

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==About this Structure==

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[[Category: Griffith, J P.]]

[[Category: Rossmann, M G.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 09~~:29:53 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:03:36 2008''

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-[[Image:2ldx.jpg|left|200px]]
+{{Seed}}
+[[Image:2ldx.png|left|200px]]
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 {{STRUCTURE_2ldx|  PDB=2ldx  |  SCENE=  }}
-'''CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_2443489}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 2443489 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_2443489}}
 ==About this Structure==
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 [[Category: Griffith, J P.]]
 [[Category: Rossmann, M G.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:29:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:03:36 2008''