2ldx: Difference between revisions

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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"
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 />


==Overview==
==CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4==
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.
<StructureSection load='2ldx' size='340' side='right'caption='[[2ldx]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ldx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ldx 1ldx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.96&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ldx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldx OCA], [https://pdbe.org/2ldx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldx RCSB], [https://www.ebi.ac.uk/pdbsum/2ldx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LDHC_MOUSE LDHC_MOUSE] Possible role in sperm motility (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ld/2ldx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ldx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:2443489</ref>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2443489 2443489]
</div>
[[Category: L-lactate dehydrogenase]]
<div class="pdbe-citations 2ldx" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Griffith JP]]
[[Category: Griffith, J.P.]]
[[Category: Rossmann MG]]
[[Category: Rossmann, M.G.]]
[[Category: oxidoreductase(choh(d)-nad(a))]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:41:41 2007''

Latest revision as of 12:44, 26 July 2023

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

2ldx, resolution 2.96Å

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