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8dir
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The complex structure between human IgG1 Fc and its high affinity receptor FcgRI H174R variant== |
| + | <StructureSection load='8dir' size='340' side='right'caption='[[8dir]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8dir]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DIR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8dir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dir OCA], [https://pdbe.org/8dir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dir RCSB], [https://www.ebi.ac.uk/pdbsum/8dir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dir ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FCGR1_HUMAN FCGR1_HUMAN] High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses.<ref>PMID:8611682</ref> <ref>PMID:9881690</ref> <ref>PMID:10397749</ref> <ref>PMID:10514529</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Understanding the molecular mechanism underlying the hierarchic binding between FcgammaRs and IgG antibodies is critical for therapeutic antibody engineering and FcgammaR functions. The recent determination of crystal structures of FcgammaRI-Fc complexes, however, resulted in two controversial mechanisms for the high affinity receptor binding to IgG. Here, we describe high resolution structures of a bovine FG-loop variant of FcgammaRI in complex with the Fc fragment of IgG(1) crystallized in three different conditions at neutral pH, confirming the characteristic FG loop-Fc interaction is critical to the high affinity immunoglobulin binding. We showed that the FcgammaRI D2-domain FG-loop functioned as a pH-sensing switch for IgG binding. Further live cell imaging of FcgammaRI-mediated internalization of immune complexes showed a pH sensitive temporal-spatial antibody-antigen uptake and release. Taken together, we demonstrate that the structures of FcgammaRI-Fc crystallized at neutral and acidic pH, respectively, represent the high and low affinity binding states of the receptor for IgG uptake and release. These results support a role for FcgammaRI in antigen delivery, highlight the importance of Fc glycan in antibody binding to the high affinity receptor and provide new insights to future antibody engineering. | ||
| - | + | FcgammaRI FG-loop functions as a pH sensitive switch for IgG binding and release.,Lu J, Spencer M, Zou Z, Traver M, Brzostowski J, Sun PD Front Immunol. 2023 Feb 6;14:1100499. doi: 10.3389/fimmu.2023.1100499. , eCollection 2023. PMID:36814926<ref>PMID:36814926</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8dir" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lu | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lu J]] | ||
| + | [[Category: Sun PD]] | ||
Revision as of 06:54, 10 May 2023
The complex structure between human IgG1 Fc and its high affinity receptor FcgRI H174R variant
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