Crystal structure of the human leukocyte Fc receptor, FcγRIIa
Fcγ receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three–dimensional structure of the extracellular portion of human FcγRIIa to 2.0 Å resolution providing a structural basis for the unique functions of the leukocyte FcR family. The re...
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Veröffentlicht in: | Nature Structural Biology 1999-05, Vol.6 (5), p.437-442 |
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creator | Hogarth, P. Mark Maxwell, Kelly F Powell, Maree S Hulett, Mark D Barton, Peter A McKenzie, Ian F. C Garrett, Thomas P.J |
description | Fcγ receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three–dimensional structure of the extracellular portion of human FcγRIIa to 2.0 Å resolution providing a structural basis for the unique functions of the leukocyte FcR family. The receptor is composed of two immunoglobulin domains and arranged to expose the ligand–binding site at one end of domain 2. Using alanine mutants we find that the binding sites for IgG1 and 2 are similar but the relative importance of specific regions on the receptor varies. In crystals, FcγRIIa molecules associate to resemble V
L
V
H
dimers, suggesting that two FcγRIIa molecules could cooperate to bind IgG in an asymmetric manner. |
doi_str_mv | 10.1038/8241 |
format | Article |
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L
V
H
dimers, suggesting that two FcγRIIa molecules could cooperate to bind IgG in an asymmetric manner.</description><identifier>ISSN: 1072-8368</identifier><identifier>EISSN: 2331-365X</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/8241</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; letter ; Life Sciences ; Membrane Biology ; Protein Structure</subject><ispartof>Nature Structural Biology, 1999-05, Vol.6 (5), p.437-442</ispartof><rights>Nature America Inc. 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/8241$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/8241$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,27913,27914,41477,42546,51308</link.rule.ids></links><search><creatorcontrib>Hogarth, P. Mark</creatorcontrib><creatorcontrib>Maxwell, Kelly F</creatorcontrib><creatorcontrib>Powell, Maree S</creatorcontrib><creatorcontrib>Hulett, Mark D</creatorcontrib><creatorcontrib>Barton, Peter A</creatorcontrib><creatorcontrib>McKenzie, Ian F. C</creatorcontrib><creatorcontrib>Garrett, Thomas P.J</creatorcontrib><title>Crystal structure of the human leukocyte Fc receptor, FcγRIIa</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><description>Fcγ receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three–dimensional structure of the extracellular portion of human FcγRIIa to 2.0 Å resolution providing a structural basis for the unique functions of the leukocyte FcR family. The receptor is composed of two immunoglobulin domains and arranged to expose the ligand–binding site at one end of domain 2. Using alanine mutants we find that the binding sites for IgG1 and 2 are similar but the relative importance of specific regions on the receptor varies. In crystals, FcγRIIa molecules associate to resemble V
L
V
H
dimers, suggesting that two FcγRIIa molecules could cooperate to bind IgG in an asymmetric manner.</description><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>letter</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Protein Structure</subject><issn>1072-8368</issn><issn>2331-365X</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNot0M1KAzEQB_AgCtbWd4gHPbmaSbLZzUWQ4kehIIiCt5BNZ23rNlvzcehz-R4-k1vqaRj48WfmT8gE2A0wUd_WXMIRGXEhoBCq_DgmI2AVL2qh6lNyFuOaMZCS6RG5m4ZdTLajMYXsUg5I-5amJdJl3lhPO8xfvdslpI-OBnS4TX24Hpbfn9fZzE7ISWu7iOf_c0zeHx_eps_F_OVpNr2fF55LlooSmLUagdcKdNVYgUoCVy04jq1zfCGFdRUw3fLSlY43slUWq5IzAKkWjRiTq0PuNvTfGWMym1V02HXWY5-jgYprLaUa4OUBxm1Y-U8MZt3n4IfbDDCzb8fs2xncxcF5u3_aDHpjw8742LBSayNFJf4AIGthXQ</recordid><startdate>19990501</startdate><enddate>19990501</enddate><creator>Hogarth, P. Mark</creator><creator>Maxwell, Kelly F</creator><creator>Powell, Maree S</creator><creator>Hulett, Mark D</creator><creator>Barton, Peter A</creator><creator>McKenzie, Ian F. C</creator><creator>Garrett, Thomas P.J</creator><general>Nature Publishing Group US</general><scope>7T5</scope><scope>H94</scope></search><sort><creationdate>19990501</creationdate><title>Crystal structure of the human leukocyte Fc receptor, FcγRIIa</title><author>Hogarth, P. Mark ; Maxwell, Kelly F ; Powell, Maree S ; Hulett, Mark D ; Barton, Peter A ; McKenzie, Ian F. C ; Garrett, Thomas P.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-n240t-510aa9e1286197ba3e64126f1c2efcc2d43ac7109f25c5c2b4f6ae75201146db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>letter</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Protein Structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hogarth, P. Mark</creatorcontrib><creatorcontrib>Maxwell, Kelly F</creatorcontrib><creatorcontrib>Powell, Maree S</creatorcontrib><creatorcontrib>Hulett, Mark D</creatorcontrib><creatorcontrib>Barton, Peter A</creatorcontrib><creatorcontrib>McKenzie, Ian F. C</creatorcontrib><creatorcontrib>Garrett, Thomas P.J</creatorcontrib><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hogarth, P. Mark</au><au>Maxwell, Kelly F</au><au>Powell, Maree S</au><au>Hulett, Mark D</au><au>Barton, Peter A</au><au>McKenzie, Ian F. C</au><au>Garrett, Thomas P.J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the human leukocyte Fc receptor, FcγRIIa</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><date>1999-05-01</date><risdate>1999</risdate><volume>6</volume><issue>5</issue><spage>437</spage><epage>442</epage><pages>437-442</pages><issn>1072-8368</issn><eissn>2331-365X</eissn><eissn>1545-9985</eissn><abstract>Fcγ receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three–dimensional structure of the extracellular portion of human FcγRIIa to 2.0 Å resolution providing a structural basis for the unique functions of the leukocyte FcR family. The receptor is composed of two immunoglobulin domains and arranged to expose the ligand–binding site at one end of domain 2. Using alanine mutants we find that the binding sites for IgG1 and 2 are similar but the relative importance of specific regions on the receptor varies. In crystals, FcγRIIa molecules associate to resemble V
L
V
H
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subjects | Biochemistry Biological Microscopy Biomedical and Life Sciences letter Life Sciences Membrane Biology Protein Structure |
title | Crystal structure of the human leukocyte Fc receptor, FcγRIIa |
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