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| | ==Crystal structure of Fc RI and its implication to high affinity immunoglobulin G binding== | | ==Crystal structure of Fc RI and its implication to high affinity immunoglobulin G binding== |
| - | <StructureSection load='3rjd' size='340' side='right' caption='[[3rjd]], [[Resolution|resolution]] 2.65Å' scene=''> | + | <StructureSection load='3rjd' size='340' side='right'caption='[[3rjd]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rjd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RJD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rjd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RJD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCGR1A, FCG1, FCGR1, IGFR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCGR1A, FCG1, FCGR1, IGFR1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rjd OCA], [http://pdbe.org/3rjd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rjd RCSB], [http://www.ebi.ac.uk/pdbsum/3rjd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rjd 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=3rjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rjd OCA], [https://pdbe.org/3rjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rjd RCSB], [https://www.ebi.ac.uk/pdbsum/3rjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rjd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Lu, J]] | | [[Category: Lu, J]] |
| | [[Category: Sun, P D]] | | [[Category: Sun, P D]] |
| | [[Category: Immune system]] | | [[Category: Immune system]] |
| Structural highlights
3rjd is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , |
| Gene: | FCGR1A, FCG1, FCGR1, IGFR1 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[FCGR1_HUMAN] High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses.[1] [2] [3] [4]
Publication Abstract from PubMed
Fcgamma receptors (FcgammaRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG). Among them, FcgammaRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy. Here we report the first crystal structure of an FcgammaRI with all three extracellular Ig-like domains (designated as D1, D2, and D3). The structure shows that, first, FcgammaRI has an acute D1-D2 hinge angle similar to that of FcepsilonRI but much smaller than those observed in the low affinity Fcgamma receptors. Second, the D3 domain of FcgammaRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc. Third, the replacement of FcgammaRIII FG-loop ((171)LVGSKNV(177)) with that of FcgammaRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcgammaRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement. Thus, the FcgammaRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding. The structural results support FcgammaRI binding to IgG in a similar mode as its low affinity counterparts. Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcgammaRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
Crystal structure of Fcgamma receptor I and its implication in high affinity gamma-immunoglobulin binding.,Lu J, Ellsworth JL, Hamacher N, Oak SW, Sun PD J Biol Chem. 2011 Nov 25;286(47):40608-13. Epub 2011 Sep 29. PMID:21965667[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Vugt MJ, Heijnen AF, Capel PJ, Park SY, Ra C, Saito T, Verbeek JS, van de Winkel JG. FcR gamma-chain is essential for both surface expression and function of human Fc gamma RI (CD64) in vivo. Blood. 1996 May 1;87(9):3593-9. PMID:8611682
- ↑ Ernst LK, Duchemin AM, Miller KL, Anderson CL. Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts. Mol Immunol. 1998 Oct;35(14-15):943-54. PMID:9881690
- ↑ van Vugt MJ, Kleijmeer MJ, Keler T, Zeelenberg I, van Dijk MA, Leusen JH, Geuze HJ, van de Winkel JG. The FcgammaRIa (CD64) ligand binding chain triggers major histocompatibility complex class II antigen presentation independently of its associated FcR gamma-chain. Blood. 1999 Jul 15;94(2):808-17. PMID:10397749
- ↑ Edberg JC, Yee AM, Rakshit DS, Chang DJ, Gokhale JA, Indik ZK, Schreiber AD, Kimberly RP. The cytoplasmic domain of human FcgammaRIa alters the functional properties of the FcgammaRI.gamma-chain receptor complex. J Biol Chem. 1999 Oct 15;274(42):30328-33. PMID:10514529
- ↑ Lu J, Ellsworth JL, Hamacher N, Oak SW, Sun PD. Crystal structure of Fcgamma receptor I and its implication in high affinity gamma-immunoglobulin binding. J Biol Chem. 2011 Nov 25;286(47):40608-13. Epub 2011 Sep 29. PMID:21965667 doi:10.1074/jbc.M111.257550
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