Recognition of a Cell-Surface Oligosaccharide of Pathogenic Salmonella by an Antibody Fab Fragment
The 2.05 angstrom (Å) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other, car...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 1991-07, Vol.253 (5018), p.442-445 |
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description | The 2.05 angstrom (Å) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other, carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 Å deep by 7 Å wide) in an entropy-assisted association (association constant = 2.05 × 10$^5$ liters per mole, enthalpy = -20.5 ± 1.7 kilojoules per mole, and temperature times entropy = + 10.0 ± 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine~ the antigen conformation adopted in the bound state |
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A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 Å deep by 7 Å wide) in an entropy-assisted association (association constant = 2.05 × 10$^5$ liters per mole, enthalpy = -20.5 ± 1.7 kilojoules per mole, and temperature times entropy = + 10.0 ± 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine~ the antigen conformation adopted in the bound state</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1713710</identifier><identifier>PMID: 1713710</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Antibodies ; Antigen-Antibody Complex ; Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation ; Antigens ; Atoms ; Biological and medical sciences ; Carbohydrate Conformation ; Carbohydrate Sequence ; Carbohydrates ; Crystal structure ; Epitopes ; Epitopes - chemistry ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Hydrogen bonds ; Immune complexes ; Immunoglobulin Fab Fragments - chemistry ; Immunoglobulin Fab Fragments - immunology ; Immunoglobulin G - classification ; Immunoglobulin G - immunology ; Lipopolysaccharides - chemistry ; Lipopolysaccharides - immunology ; Models, Molecular ; Molecular immunology ; Molecular Sequence Data ; Molecular structure ; Molecules ; Oligosaccharides ; Oligosaccharides - chemistry ; Oligosaccharides - immunology ; Protein Conformation ; Salmonella - immunology ; Salmonella - pathogenicity ; Science ; Sugars ; X-ray crystallography</subject><ispartof>Science (American Association for the Advancement of Science), 1991-07, Vol.253 (5018), p.442-445</ispartof><rights>Copyright 1991 American Association for the Advancement of Science</rights><rights>1992 INIST-CNRS</rights><rights>COPYRIGHT 1991 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1991 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Jul 26, 1991</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c675t-30acbe465eb95d46c35e5967c340cec1cd0634c35d1635dab5acb24383bfb2e43</citedby><cites>FETCH-LOGICAL-c675t-30acbe465eb95d46c35e5967c340cec1cd0634c35d1635dab5acb24383bfb2e43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2878892$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2878892$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5070456$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1713710$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cygler, Miroslaw</creatorcontrib><creatorcontrib>Rose, David R.</creatorcontrib><creatorcontrib>Bundle, David R.</creatorcontrib><title>Recognition of a Cell-Surface Oligosaccharide of Pathogenic Salmonella by an Antibody Fab Fragment</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The 2.05 angstrom (Å) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other, carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 Å deep by 7 Å wide) in an entropy-assisted association (association constant = 2.05 × 10$^5$ liters per mole, enthalpy = -20.5 ± 1.7 kilojoules per mole, and temperature times entropy = + 10.0 ± 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine~ the antigen conformation adopted in the bound state</description><subject>Amino Acid Sequence</subject><subject>Antibodies</subject><subject>Antigen-Antibody Complex</subject><subject>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</subject><subject>Antigens</subject><subject>Atoms</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Conformation</subject><subject>Carbohydrate Sequence</subject><subject>Carbohydrates</subject><subject>Crystal structure</subject><subject>Epitopes</subject><subject>Epitopes - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Hydrogen bonds</subject><subject>Immune complexes</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin Fab Fragments - immunology</subject><subject>Immunoglobulin G - classification</subject><subject>Immunoglobulin G - immunology</subject><subject>Lipopolysaccharides - chemistry</subject><subject>Lipopolysaccharides - immunology</subject><subject>Models, Molecular</subject><subject>Molecular immunology</subject><subject>Molecular Sequence Data</subject><subject>Molecular structure</subject><subject>Molecules</subject><subject>Oligosaccharides</subject><subject>Oligosaccharides - chemistry</subject><subject>Oligosaccharides - immunology</subject><subject>Protein Conformation</subject><subject>Salmonella - immunology</subject><subject>Salmonella - pathogenicity</subject><subject>Science</subject><subject>Sugars</subject><subject>X-ray crystallography</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0lGr0zAUAOAgynVOn31RKCLqw-29SdOk7eMcbl4YTpz6GtL0tDejTa5JC-7fm7EymQwZgQRyvoTknIPQS4JvCEn4rVcajIIbkhGaEfwITQguWFwkmD5GE4wpj3OcsafomfdbjEOsoFfoauQTVH4DZRuje21NZOtIRnNo23gzuFoqiNatbqyXSt1LpyvYi6-yv7cNGK2ijWw7a4KXUbmLpIlmptelrXbRQpbRwsmmA9M_R09q2Xp4Ma5T9GPx6fv8c7xaL-_ms1WseMb6mGKpSkg5g7JgVcoVZcAKnimaYgWKqApzmobdivAwyZIFn6Q0p2VdJpDSKXp3uPfB2V8D-F502qv96wzYwYuQB8IwywJ8_1-YpTQlIXP7K9_8I7d2cCb8QiSEMk6LhAZ0fUCNbEFoU9veSRUyBE62IT21DtszQgjPM5oEHp_hYVTQaXXOfzjxgfTwu2_k4L2423y5mK5_Xkw_Li-l-XJ1Qq_PUWXbFhoQodzz9Qm_PXDlrPcOavHgdCfdThAs9u0txvYWY7-GE6_HggxlB9Vff4y_HePSK9nWThql_ZExnOE0lG2KXh3Y1vfWHcNJnuV5KOkfcf4HCA</recordid><startdate>19910726</startdate><enddate>19910726</enddate><creator>Cygler, Miroslaw</creator><creator>Rose, David R.</creator><creator>Bundle, David R.</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19910726</creationdate><title>Recognition of a Cell-Surface Oligosaccharide of Pathogenic Salmonella by an Antibody Fab Fragment</title><author>Cygler, Miroslaw ; Rose, David R. ; Bundle, David R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c675t-30acbe465eb95d46c35e5967c340cec1cd0634c35d1635dab5acb24383bfb2e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Antibodies</topic><topic>Antigen-Antibody Complex</topic><topic>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</topic><topic>Antigens</topic><topic>Atoms</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Conformation</topic><topic>Carbohydrate Sequence</topic><topic>Carbohydrates</topic><topic>Crystal structure</topic><topic>Epitopes</topic><topic>Epitopes - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Hydrogen bonds</topic><topic>Immune complexes</topic><topic>Immunoglobulin Fab Fragments - chemistry</topic><topic>Immunoglobulin Fab Fragments - immunology</topic><topic>Immunoglobulin G - classification</topic><topic>Immunoglobulin G - immunology</topic><topic>Lipopolysaccharides - chemistry</topic><topic>Lipopolysaccharides - immunology</topic><topic>Models, Molecular</topic><topic>Molecular immunology</topic><topic>Molecular Sequence Data</topic><topic>Molecular structure</topic><topic>Molecules</topic><topic>Oligosaccharides</topic><topic>Oligosaccharides - chemistry</topic><topic>Oligosaccharides - immunology</topic><topic>Protein Conformation</topic><topic>Salmonella - immunology</topic><topic>Salmonella - pathogenicity</topic><topic>Science</topic><topic>Sugars</topic><topic>X-ray crystallography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cygler, 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Cell-Surface Oligosaccharide of Pathogenic Salmonella by an Antibody Fab Fragment</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1991-07-26</date><risdate>1991</risdate><volume>253</volume><issue>5018</issue><spage>442</spage><epage>445</epage><pages>442-445</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The 2.05 angstrom (Å) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other, carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 Å deep by 7 Å wide) in an entropy-assisted association (association constant = 2.05 × 10$^5$ liters per mole, enthalpy = -20.5 ± 1.7 kilojoules per mole, and temperature times entropy = + 10.0 ± 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine~ the antigen conformation adopted in the bound state</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>1713710</pmid><doi>10.1126/science.1713710</doi><tpages>4</tpages></addata></record> |
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source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
subjects | Amino Acid Sequence Antibodies Antigen-Antibody Complex Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation Antigens Atoms Biological and medical sciences Carbohydrate Conformation Carbohydrate Sequence Carbohydrates Crystal structure Epitopes Epitopes - chemistry Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Hydrogen bonds Immune complexes Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - immunology Immunoglobulin G - classification Immunoglobulin G - immunology Lipopolysaccharides - chemistry Lipopolysaccharides - immunology Models, Molecular Molecular immunology Molecular Sequence Data Molecular structure Molecules Oligosaccharides Oligosaccharides - chemistry Oligosaccharides - immunology Protein Conformation Salmonella - immunology Salmonella - pathogenicity Science Sugars X-ray crystallography |
title | Recognition of a Cell-Surface Oligosaccharide of Pathogenic Salmonella by an Antibody Fab Fragment |
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