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1igi
From Proteopedia
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==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='1igi' size='340' side='right' caption='[[1igi]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='1igi' size='340' side='right'caption='[[1igi]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1igi]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1igi]] 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=1IGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IGI FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=1igi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1igi OCA], [https://pdbe.org/1igi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1igi RCSB], [https://www.ebi.ac.uk/pdbsum/1igi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1igi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ig/1igi_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ig/1igi_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1igi ConSurf]. |
<div style="clear:both"></div> | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[Monoclonal | + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Jeffrey | + | [[Category: Jeffrey PD]] |
| - | [[Category: Sheriff | + | [[Category: Sheriff S]] |
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Current revision
26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY
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