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<StructureSection load='7uem' size='340' side='right'caption='[[7uem]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
<StructureSection load='7uem' size='340' side='right'caption='[[7uem]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7uem]] is a 4 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6nv0 6nv0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UEM FirstGlance]. <br>
<table><tr><td colspan='2'>[[7uem]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6nv0 6nv0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UEM 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>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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]] 2.314&#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>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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=7uem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uem OCA], [https://pdbe.org/7uem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uem RCSB], [https://www.ebi.ac.uk/pdbsum/7uem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uem 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=7uem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uem OCA], [https://pdbe.org/7uem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uem RCSB], [https://www.ebi.ac.uk/pdbsum/7uem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uem 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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7uem" 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>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Christ, D]]
[[Category: Christ D]]
[[Category: Langley, D B]]
[[Category: Langley DB]]
[[Category: Alpha-galactosyl]]
[[Category: Anti-alpha-gal]]
[[Category: Antibody]]
[[Category: Immune response]]
[[Category: Immune system]]
[[Category: M86]]

Latest revision as of 10:22, 3 April 2024

Genomic and structural basis for the human anti-alpha-galactosyl antibody responseGenomic and structural basis for the human anti-alpha-galactosyl antibody response

Structural highlights

7uem is a 4 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 6nv0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.314Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7uem, resolution 2.31Å

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