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[[Image:1ghf.gif|left|200px]]
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{{STRUCTURE_1ghf|  PDB=1ghf  |  SCENE=  }}
'''ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT'''


==ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT==
<StructureSection load='1ghf' size='340' side='right'caption='[[1ghf]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ghf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHF 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]] 2.7&#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=1ghf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghf OCA], [https://pdbe.org/1ghf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghf RCSB], [https://www.ebi.ac.uk/pdbsum/1ghf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghf ProSAT]</span></td></tr>
</table>
== 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/gh/1ghf_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=1ghf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the Fab fragment of the mouse anti-anti-idiotypic monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which mimics the determinant defined by anti-human high molecular weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments of mAb GH1002 exist in the crystal as dimers related by crystallographic 2-fold axes. The interface between dyad-related Fab fragments is formed primarily by interaction of the hypervariable loops of one with the other. The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002 through their combining sites is extremely tight and intricate, closely resembling that observed in structures of id-anti-id complexes, and comparable in terms of total contact area, charge complementarity, and number of hydrogen bonds. The self-complementarity of the antibody observed here could be coincidental and thus reflect some non-specific binding capability. It might, on the other hand, be immunologically relevant and exemplify a certain degree of evolved self complementarity characteristic of antibodies participating in idiotypic cascades.


==Overview==
Crystal structure of an anti-anti-idiotype shows it to be self-complementary.,Ban N, Day J, Wang X, Ferrone S, McPherson A J Mol Biol. 1996 Feb 2;255(4):617-27. PMID:8568901<ref>PMID:8568901</ref>
The structure of the Fab fragment of the mouse anti-anti-idiotypic monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which mimics the determinant defined by anti-human high molecular weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments of mAb GH1002 exist in the crystal as dimers related by crystallographic 2-fold axes. The interface between dyad-related Fab fragments is formed primarily by interaction of the hypervariable loops of one with the other. The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002 through their combining sites is extremely tight and intricate, closely resembling that observed in structures of id-anti-id complexes, and comparable in terms of total contact area, charge complementarity, and number of hydrogen bonds. The self-complementarity of the antibody observed here could be coincidental and thus reflect some non-specific binding capability. It might, on the other hand, be immunologically relevant and exemplify a certain degree of evolved self complementarity characteristic of antibodies participating in idiotypic cascades.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHF OCA].
</div>
<div class="pdbe-citations 1ghf" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of an anti-anti-idiotype shows it to be self-complementary., Ban N, Day J, Wang X, Ferrone S, McPherson A, J Mol Biol. 1996 Feb 2;255(4):617-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8568901 8568901]
*[[Antibody 3D structures|Antibody 3D structures]]
[[Category: Ban, N.]]
*[[Sandbox 20009|Sandbox 20009]]
[[Category: Day, J.]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
[[Category: Ferrone, S.]]
== References ==
[[Category: McPherson, A.]]
<references/>
[[Category: Wang, X.]]
__TOC__
[[Category: Antibody fab fragment]]
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:33:51 2008''
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Ban N]]
[[Category: Day J]]
[[Category: Ferrone S]]
[[Category: McPherson A]]
[[Category: Wang X]]
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