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6p4c
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==HyHEL10 Fab carrying four heavy chain mutations (HyHEL10-4x): L4F, Y33H, S56N, and Y58F== | |
| + | <StructureSection load='6p4c' size='340' side='right'caption='[[6p4c]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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'>[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> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0E4B213_MOUSE A0A0E4B213_MOUSE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:32855302</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6p4c" style="background-color:#fffaf0;"></div> |
| - | [[Category: Christ | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Christ D]] | ||
| + | [[Category: Langley DB]] | ||
Current revision
HyHEL10 Fab carrying four heavy chain mutations (HyHEL10-4x): L4F, Y33H, S56N, and Y58F
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