6p4b: Difference between revisions

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<StructureSection load='6p4b' size='340' side='right'caption='[[6p4b]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6p4b' size='340' side='right'caption='[[6p4b]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6p4b]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] 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=6P4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P4B FirstGlance]. <br>
<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]] 1.9&#8491;</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]] 1.9&#8491;</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&reg;/PubMed&reg;, 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]]

Latest revision as of 11:13, 17 October 2024

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)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)

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

6p4b, resolution 1.90Å

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