6p4b
From Proteopedia
(Difference between revisions)
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<StructureSection load='6p4b' size='340' side='right'caption='[[6p4b]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6p4b' size='340' side='right'caption='[[6p4b]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P4B 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]] 1.9Å</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]] 1.9Å</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='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=6p4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4b OCA], [https://pdbe.org/6p4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p4b RCSB], [https://www.ebi.ac.uk/pdbsum/6p4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4b 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=6p4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4b OCA], [https://pdbe.org/6p4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p4b RCSB], [https://www.ebi.ac.uk/pdbsum/6p4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4b ProSAT]</span></td></tr> | ||
</table> | </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> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6p4b" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Mus musculus]] | ||
[[Category: Christ D]] | [[Category: Christ D]] | ||
[[Category: Langley DB]] | [[Category: Langley DB]] | ||
Current revision
HyHEL10 fab variant HyHEL10-4x (heavy chain mutations L4F, Y33H, S56N, and Y58F) bound to hen egg lysozyme variant HEL2x-flex (mutations R21Q, R73E, C76S, and C94S)
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