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| | <StructureSection load='6p4c' size='340' side='right'caption='[[6p4c]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='6p4c' size='340' side='right'caption='[[6p4c]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6p4c]] 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=6P4C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6P4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6p4c]] 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=6P4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P4C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6p4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4c OCA], [http://pdbe.org/6p4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p4c RCSB], [http://www.ebi.ac.uk/pdbsum/6p4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4c ProSAT]</span></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=6p4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4c OCA], [https://pdbe.org/6p4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p4c RCSB], [https://www.ebi.ac.uk/pdbsum/6p4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0E4B213_MOUSE A0A0E4B213_MOUSE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Christ, D]] | + | [[Category: Christ D]] |
| - | [[Category: Langley, D B]] | + | [[Category: Langley DB]] |
| - | [[Category: Fab]]
| + | |
| - | [[Category: Hyhel10]]
| + | |
| - | [[Category: Hyhel10-4x]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Lysozyme-binder]]
| + | |
| Structural highlights
Function
A0A0E4B213_MOUSE
Publication Abstract from PubMed
Conformational diversity and self-cross-reactivity of antigens have been correlated with evasion from neutralizing antibody responses. We utilized single cell B cell sequencing, biolayer interferometry and X-ray crystallography to trace mutation selection pathways where the antibody response must resolve cross-reactivity between foreign and self-proteins bearing near-identical contact surfaces, but differing in conformational flexibility. Recurring antibody mutation trajectories mediate long-range rearrangements of framework (FW) and complementarity determining regions (CDRs) that increase binding site conformational diversity. These antibody mutations decrease affinity for self-antigen 19-fold and increase foreign affinity 67-fold, to yield a more than 1,250-fold increase in binding discrimination. These results demonstrate how conformational diversity in antigen and antibody does not act as a barrier, as previously suggested, but rather facilitates high affinity and high discrimination between foreign and self.
Conformational diversity facilitates antibody mutation trajectories and discrimination between foreign and self-antigens.,Burnett DL, Schofield P, Langley DB, Jackson J, Bourne K, Wilson E, Porebski BT, Buckle AM, Brink R, Goodnow CC, Christ D Proc Natl Acad Sci U S A. 2020 Sep 8;117(36):22341-22350. doi:, 10.1073/pnas.2005102117. Epub 2020 Aug 27. PMID:32855302[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burnett DL, Schofield P, Langley DB, Jackson J, Bourne K, Wilson E, Porebski BT, Buckle AM, Brink R, Goodnow CC, Christ D. Conformational diversity facilitates antibody mutation trajectories and discrimination between foreign and self-antigens. Proc Natl Acad Sci U S A. 2020 Sep 8;117(36):22341-22350. doi:, 10.1073/pnas.2005102117. Epub 2020 Aug 27. PMID:32855302 doi:http://dx.doi.org/10.1073/pnas.2005102117
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