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[[Image:1igj.gif|left|200px]]
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{{STRUCTURE_1igj|  PDB=1igj  |  SCENE=  }}
'''26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY'''


==26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY==
<StructureSection load='1igj' size='340' side='right'caption='[[1igj]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1igj]] is a 4 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=1IGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IGJ 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGX:DIGOXIN'>DGX</scene></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=1igj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1igj OCA], [https://pdbe.org/1igj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1igj RCSB], [https://www.ebi.ac.uk/pdbsum/1igj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1igj 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/ig/1igj_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1igj ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the three-dimensional structures of the antigen-binding fragment of the anti-digoxin monoclonal antibody 26-10 in the uncomplexed state at 2.7 A resolution and as a complex with digoxin at 2.5 A resolution. Neither the antibody nor digoxin undergoes any significant conformational changes upon forming the complex. Digoxin interacts primarily with the antibody heavy chain and is oriented such that the carbohydrate groups are exposed to solvent and the lactone ring is buried in a deep pocket at the bottom of the combining site. Despite extensive interactions between antibody and antigen, no hydrogen bonds or salt links are formed between 26-10 and digoxin. Thus the 26-10-digoxin complex is unique among the known three-dimensional structures of antibody-antigen complexes in that specificity and high affinity arise primarily from shape complementarity.


==Overview==
26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity.,Jeffrey PD, Strong RK, Sieker LC, Chang CY, Campbell RL, Petsko GA, Haber E, Margolies MN, Sheriff S Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10310-4. PMID:8234291<ref>PMID:8234291</ref>
We have determined the three-dimensional structures of the antigen-binding fragment of the anti-digoxin monoclonal antibody 26-10 in the uncomplexed state at 2.7 A resolution and as a complex with digoxin at 2.5 A resolution. Neither the antibody nor digoxin undergoes any significant conformational changes upon forming the complex. Digoxin interacts primarily with the antibody heavy chain and is oriented such that the carbohydrate groups are exposed to solvent and the lactone ring is buried in a deep pocket at the bottom of the combining site. Despite extensive interactions between antibody and antigen, no hydrogen bonds or salt links are formed between 26-10 and digoxin. Thus the 26-10-digoxin complex is unique among the known three-dimensional structures of antibody-antigen complexes in that specificity and high affinity arise primarily from shape complementarity.


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


==Reference==
==See Also==
26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity., Jeffrey PD, Strong RK, Sieker LC, Chang CY, Campbell RL, Petsko GA, Haber E, Margolies MN, Sheriff S, Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10310-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8234291 8234291]
*[[Antibody 3D structures|Antibody 3D structures]]
[[Category: Protein complex]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
[[Category: Jeffrey, P D.]]
== References ==
[[Category: Sheriff, S.]]
<references/>
[[Category: Immunoglobulin]]
__TOC__
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:58:28 2008''
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Jeffrey PD]]
[[Category: Sheriff S]]
Retrieved from "https://proteopedia.org/1igj"