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| | <StructureSection load='3mbx' size='340' side='right'caption='[[3mbx]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='3mbx' size='340' side='right'caption='[[3mbx]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mbx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MBX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MBX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mbx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MBX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l7e|3l7e]]</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=3mbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mbx OCA], [https://pdbe.org/3mbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mbx RCSB], [https://www.ebi.ac.uk/pdbsum/3mbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mbx ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mbx OCA], [http://pdbe.org/3mbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mbx RCSB], [http://www.ebi.ac.uk/pdbsum/3mbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mbx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gilliland, G L]] | + | [[Category: Gilliland GL]] |
| - | [[Category: Obmolova, G]] | + | [[Category: Obmolova G]] |
| - | [[Category: Teplyakov, A]] | + | [[Category: Teplyakov A]] |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunoglobulin fold]]
| + | |
| - | [[Category: Monoclonal antibody]]
| + | |
| Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A chimeric antibody was constructed from two unrelated antibodies by combining their heavy and light chains. The "double chimera" consists of the mouse variable regions of different specificity (IL-13 and EMMPRIN) and the constant regions of different origin (mouse and human). The Fab fragment of this chimeric antibody was expressed in mammalian cells, and the crystal structure was determined at 1.6A resolution. Despite a large number of amino acid substitutions in the double chimera with respect to the parent antibodies, the heavy and light chains associate into a stable molecule. Comparison to the structure of one of the parent antibodies reveals that the variable domain interface, as well as the conformation of antigen-binding loops, is preserved without major rearrangements due to conservation of amino acids in key positions. Comparison to the structures of the all-human and all-mouse constant domains indicates a remarkable plasticity of the inter-chain interface that can tolerate residue relocations of up to 6A.
On the domain pairing in chimeric antibodies.,Teplyakov A, Obmolova G, Carton JM, Gao W, Zhao Y, Gilliland GL Mol Immunol. 2010 Aug;47(14):2422-6. PMID:20554002[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Teplyakov A, Obmolova G, Carton JM, Gao W, Zhao Y, Gilliland GL. On the domain pairing in chimeric antibodies. Mol Immunol. 2010 Aug;47(14):2422-6. PMID:20554002 doi:10.1016/j.molimm.2010.05.002
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