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Three-Dimensional Structure of a Human Immunoglobulin With a Hinge Deletion
X-ray analysis at 3.2-Å resolution revealed that the Mcg IgG1 (λ chain) immunoglobulin is a compact T-shaped molecule. Because of the hinge deletion, the Fc fragment lobe is pulled tightly upward into the junction of the Fab arms. Along the molecular twofold axis, the Fab arms are joined by an inter...
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| Published in: | Proceedings of the National Academy of Sciences - PNAS 1993-05, Vol.90 (9), p.4271-4275 |
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| container_end_page | 4275 |
| container_issue | 9 |
| container_start_page | 4271 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 90 |
| creator | Guddat, Luke W. Herron, James N. Edmundson, Allen B. |
| description | X-ray analysis at 3.2-Å resolution revealed that the Mcg IgG1 (λ chain) immunoglobulin is a compact T-shaped molecule. Because of the hinge deletion, the Fc fragment lobe is pulled tightly upward into the junction of the Fab arms. Along the molecular twofold axis, the Fab arms are joined by an interchain disulfide bond between the two light chains. The antigen combining sites consist of large irregular cavities at the tips of the Fab regions. Potential complement (C1q) binding sites on Fc are sterically shielded by the Fab arms, but putative attachment sites are accessible for docking with the FcRI receptor on human monocytes and with protein A of Staphylococcus aureus. |
| doi_str_mv | 10.1073/pnas.90.9.4271 |
| format | article |
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Because of the hinge deletion, the Fc fragment lobe is pulled tightly upward into the junction of the Fab arms. Along the molecular twofold axis, the Fab arms are joined by an interchain disulfide bond between the two light chains. The antigen combining sites consist of large irregular cavities at the tips of the Fab regions. Potential complement (C1q) binding sites on Fc are sterically shielded by the Fab arms, but putative attachment sites are accessible for docking with the FcRI receptor on human monocytes and with protein A of Staphylococcus aureus.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.90.9.4271</identifier><identifier>PMID: 8483943</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Antibodies ; Antibodies, immunoglobulins ; Atoms ; Binding sites ; Binding Sites, Antibody ; Biochemistry ; Biological and medical sciences ; Carbohydrate Conformation ; Complement C1q - metabolism ; Dimers ; Disulfides ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Immunity (Disease) ; Immunoglobulin Fab Fragments - chemistry ; Immunoglobulin Fab Fragments - genetics ; Immunoglobulin Fc Fragments - chemistry ; Immunoglobulin G - chemistry ; Immunoglobulin G - classification ; Immunoglobulin G - genetics ; Immunoglobulin lambda-Chains - chemistry ; Immunoglobulin lambda-Chains - genetics ; Immunoglobulins ; Medical research ; Models, Molecular ; Molecular chains ; Molecular immunology ; Molecular Sequence Data ; Molecules ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Deletion ; Structure ; Tunnels ; Tyrosine ; X-Ray Diffraction - methods</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1993-05, Vol.90 (9), p.4271-4275</ispartof><rights>Copyright 1993 The National Academy of Sciences of the United States of America</rights><rights>1993 INIST-CNRS</rights><rights>Copyright National Academy of Sciences May 1, 1993</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4361-346cd96bb5050cb518a99a4237e302417e87d716e8c6f6b546b472ffb05943a33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/90/9.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2361934$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2361934$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793,58238,58471</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4791806$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8483943$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Guddat, Luke W.</creatorcontrib><creatorcontrib>Herron, James N.</creatorcontrib><creatorcontrib>Edmundson, Allen B.</creatorcontrib><title>Three-Dimensional Structure of a Human Immunoglobulin With a Hinge Deletion</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>X-ray analysis at 3.2-Å resolution revealed that the Mcg IgG1 (λ chain) immunoglobulin is a compact T-shaped molecule. Because of the hinge deletion, the Fc fragment lobe is pulled tightly upward into the junction of the Fab arms. Along the molecular twofold axis, the Fab arms are joined by an interchain disulfide bond between the two light chains. The antigen combining sites consist of large irregular cavities at the tips of the Fab regions. Potential complement (C1q) binding sites on Fc are sterically shielded by the Fab arms, but putative attachment sites are accessible for docking with the FcRI receptor on human monocytes and with protein A of Staphylococcus aureus.</description><subject>Amino Acid Sequence</subject><subject>Antibodies</subject><subject>Antibodies, immunoglobulins</subject><subject>Atoms</subject><subject>Binding sites</subject><subject>Binding Sites, Antibody</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Conformation</subject><subject>Complement C1q - metabolism</subject><subject>Dimers</subject><subject>Disulfides</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immunity (Disease)</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin Fab Fragments - genetics</subject><subject>Immunoglobulin Fc Fragments - chemistry</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin G - classification</subject><subject>Immunoglobulin G - genetics</subject><subject>Immunoglobulin lambda-Chains - chemistry</subject><subject>Immunoglobulin lambda-Chains - genetics</subject><subject>Immunoglobulins</subject><subject>Medical research</subject><subject>Models, Molecular</subject><subject>Molecular chains</subject><subject>Molecular immunology</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Deletion</subject><subject>Structure</subject><subject>Tunnels</subject><subject>Tyrosine</subject><subject>X-Ray Diffraction - methods</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNqNkUuLFDEUhQtRxnZ060qhEHFXZV6VB7iReTiDAy4ccRlS6VR3mlTSJhXRf2-KbotWXLjK4nzn3nNzquo5BC0EDL_de5VaAVrREsTgg2oFgYANJQI8rFYAINZwgsjj6klKOwCA6Dg4q8444VgQvKo-3m-jMc2lHY1PNnjl6s9TzHrK0dRhqFV9k0fl69txzD5sXOizs77-aqftrFm_MfWlcWYq3qfVo0G5ZJ4d3_Pqy_XV_cVNc_fpw-3F-7tGE0xhgwnVa0H7vgMd0H0HuRJCEYSZwQARyAxnawap4ZoOtO8I7QlDw9CDrkRWGJ9X7w5z97kfzVobP0Xl5D7aUcWfMigr_1S83cpN-C4JJZwX-5ujPYZv2aRJjjZp45zyJuQkWccQwv8BQsoEJGwGX_0F7kKO5S-TRADijmLaFag9QDqGlKIZlsAQyLlKOVcpBZBCzlUWw8vTMxf82F3RXx91lbRyQ1Re27RgpITjgJ5cMY__rS5r5JCdm8yP6WTfP8GivzjouzSFuACodCowwb8AzsjG6A</recordid><startdate>19930501</startdate><enddate>19930501</enddate><creator>Guddat, Luke W.</creator><creator>Herron, James N.</creator><creator>Edmundson, Allen B.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19930501</creationdate><title>Three-Dimensional Structure of a Human Immunoglobulin With a Hinge Deletion</title><author>Guddat, Luke W. ; Herron, James N. ; Edmundson, Allen B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4361-346cd96bb5050cb518a99a4237e302417e87d716e8c6f6b546b472ffb05943a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Antibodies</topic><topic>Antibodies, immunoglobulins</topic><topic>Atoms</topic><topic>Binding sites</topic><topic>Binding Sites, Antibody</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Conformation</topic><topic>Complement C1q - metabolism</topic><topic>Dimers</topic><topic>Disulfides</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immunity (Disease)</topic><topic>Immunoglobulin Fab Fragments - chemistry</topic><topic>Immunoglobulin Fab Fragments - genetics</topic><topic>Immunoglobulin Fc Fragments - chemistry</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin G - classification</topic><topic>Immunoglobulin G - genetics</topic><topic>Immunoglobulin lambda-Chains - chemistry</topic><topic>Immunoglobulin lambda-Chains - genetics</topic><topic>Immunoglobulins</topic><topic>Medical research</topic><topic>Models, Molecular</topic><topic>Molecular chains</topic><topic>Molecular immunology</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Sequence Deletion</topic><topic>Structure</topic><topic>Tunnels</topic><topic>Tyrosine</topic><topic>X-Ray Diffraction - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guddat, Luke W.</creatorcontrib><creatorcontrib>Herron, James N.</creatorcontrib><creatorcontrib>Edmundson, Allen B.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guddat, Luke W.</au><au>Herron, James N.</au><au>Edmundson, Allen B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-Dimensional Structure of a Human Immunoglobulin With a Hinge Deletion</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1993-05-01</date><risdate>1993</risdate><volume>90</volume><issue>9</issue><spage>4271</spage><epage>4275</epage><pages>4271-4275</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>X-ray analysis at 3.2-Å resolution revealed that the Mcg IgG1 (λ chain) immunoglobulin is a compact T-shaped molecule. Because of the hinge deletion, the Fc fragment lobe is pulled tightly upward into the junction of the Fab arms. Along the molecular twofold axis, the Fab arms are joined by an interchain disulfide bond between the two light chains. The antigen combining sites consist of large irregular cavities at the tips of the Fab regions. Potential complement (C1q) binding sites on Fc are sterically shielded by the Fab arms, but putative attachment sites are accessible for docking with the FcRI receptor on human monocytes and with protein A of Staphylococcus aureus.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8483943</pmid><doi>10.1073/pnas.90.9.4271</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1993-05, Vol.90 (9), p.4271-4275 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_46488 |
| source | NCBI_PubMed Central（免费）; JSTOR |
| subjects | Amino Acid Sequence Antibodies Antibodies, immunoglobulins Atoms Binding sites Binding Sites, Antibody Biochemistry Biological and medical sciences Carbohydrate Conformation Complement C1q - metabolism Dimers Disulfides Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunity (Disease) Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - genetics Immunoglobulin Fc Fragments - chemistry Immunoglobulin G - chemistry Immunoglobulin G - classification Immunoglobulin G - genetics Immunoglobulin lambda-Chains - chemistry Immunoglobulin lambda-Chains - genetics Immunoglobulins Medical research Models, Molecular Molecular chains Molecular immunology Molecular Sequence Data Molecules Protein Structure, Secondary Protein Structure, Tertiary Sequence Deletion Structure Tunnels Tyrosine X-Ray Diffraction - methods |
| title | Three-Dimensional Structure of a Human Immunoglobulin With a Hinge Deletion |
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