7uen
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7uen]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6nuy 6nuy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UEN FirstGlance]. <br> | <table><tr><td colspan='2'>[[7uen]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6nuy 6nuy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UEN FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 1.55Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7uen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uen OCA], [https://pdbe.org/7uen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uen RCSB], [https://www.ebi.ac.uk/pdbsum/7uen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uen 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=7uen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uen OCA], [https://pdbe.org/7uen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uen RCSB], [https://www.ebi.ac.uk/pdbsum/7uen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uen ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Humans lack the capacity to produce the Galalpha1-3Galbeta1-4GlcNAc (alpha-gal) glycan, and produce anti-alpha-gal antibodies upon exposure to the carbohydrate on a diverse set of immunogens, including commensal gut bacteria, malaria parasites, cetuximab, and tick proteins. Here we use X-ray crystallographic analysis of antibodies from alpha-gal knockout mice and humans in complex with the glycan to reveal a common binding motif, centered on a germline-encoded tryptophan residue at Kabat position 33 (W33) of the complementarity-determining region of the variable heavy chain (CDRH1). Immunoglobulin sequencing of anti-alpha-gal B cells in healthy humans and tick-induced mammalian meat anaphylaxis patients revealed preferential use of heavy chain germline IGHV3-7, encoding W33, among an otherwise highly polyclonal antibody response. Antigen binding was critically dependent on the presence of the germline-encoded W33 residue for all of the analyzed antibodies; moreover, introduction of the W33 motif into naive IGHV3-23 antibody phage libraries enabled the rapid selection of alpha-gal binders. Our results outline structural and genetic factors that shape the human anti-alpha-galactosyl antibody response, and provide a framework for future therapeutics development. | ||
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| - | Genetic and structural basis of the human anti-alpha-galactosyl antibody response.,Langley DB, Schofield P, Nevoltris D, Jackson J, Jackson KJL, Peters TJ, Burk M, Matthews JM, Basten A, Goodnow CC, van Nunen S, Reed JH, Christ D Proc Natl Acad Sci U S A. 2022 Jul 12;119(28):e2123212119. doi:, 10.1073/pnas.2123212119. Epub 2022 Jul 8. PMID:35867757<ref>PMID:35867757</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7uen" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | *[[Antibody 3D structures|Antibody 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Genetic and structural basis of the human anti-alpha-galactosyl antibody response
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