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| | ==IgG1 Fc-FcgammaRI ecd complex== | | ==IgG1 Fc-FcgammaRI ecd complex== |
| - | <StructureSection load='4zne' size='340' side='right' caption='[[4zne]], [[Resolution|resolution]] 2.42Å' scene=''> | + | <StructureSection load='4zne' size='340' side='right'caption='[[4zne]], [[Resolution|resolution]] 2.42Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zne]] is a 3 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=4ZNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZNE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zne]] 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=4ZNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZNE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]), IGHG1 ([http://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'>[https://proteopedia.org/fgij/fg.htm?mol=4zne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zne OCA], [https://pdbe.org/4zne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zne RCSB], [https://www.ebi.ac.uk/pdbsum/4zne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zne ProSAT]</span></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=4zne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zne OCA], [http://pdbe.org/4zne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zne RCSB], [http://www.ebi.ac.uk/pdbsum/4zne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zne ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/IGHG1_HUMAN IGHG1_HUMAN]] Defects in IGHG1 are a cause of multiple myeloma (MM) [MIM:[http://omim.org/entry/254500 254500]]. MM is a malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. Note=A chromosomal aberration involving IGHG1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus. Translocation t(11;14)(q13;q32) with CCND1; translocation t(4;14)(p16.3;q32.3) with FGFR3; translocation t(6;14)(p25;q32) with IRF4. | |
| | == 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Acqua, W F.Dall]] | + | [[Category: Large Structures]] |
| - | [[Category: Oganesyan, V Y]] | + | [[Category: Dall'Acqua WF]] |
| - | [[Category: Antibody]] | + | [[Category: Oganesyan VY]] |
| - | [[Category: Constant region]]
| + | |
| - | [[Category: High affinity]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Receptor]]
| + | |
| Structural highlights
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
The three-dimensional structure of a human IgG1 Fc fragment bound to wild-type human FcgammaRI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 A using molecular replacement; this is the highest resolution achieved for an unmutated FcgammaRI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of FcgammaRI. It also explains the long-known major energetic contribution of the Fc `LLGG' motif at positions 234-237, and particularly of Leu235, via a `lock-and-key' mechanism. Finally, a previously held belief is corrected and a differing view is offered on the recently proposed direct role of Fc carbohydrates in the corresponding interaction. Structural evidence is provided that such glycan-related effects are strictly indirect.
Structural insights into the interaction of human IgG1 with FcgammaRI: no direct role of glycans in binding.,Oganesyan V, Mazor Y, Yang C, Cook KE, Woods RM, Ferguson A, Bowen MA, Martin T, Zhu J, Wu H, Dall'Acqua WF Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2354-61. doi:, 10.1107/S1399004715018015. Epub 2015 Oct 31. PMID:26527150[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
- ↑ Oganesyan V, Mazor Y, Yang C, Cook KE, Woods RM, Ferguson A, Bowen MA, Martin T, Zhu J, Wu H, Dall'Acqua WF. Structural insights into the interaction of human IgG1 with FcgammaRI: no direct role of glycans in binding. Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2354-61. doi:, 10.1107/S1399004715018015. Epub 2015 Oct 31. PMID:26527150 doi:http://dx.doi.org/10.1107/S1399004715018015
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