Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state
The structures, obtained by X-ray crystallography, of the binding sites of catalytic antibodies raised to bind different phosphonates are compared. Although the amino acid sequences differ, all exhibit a tetrahedral array of hydrogen bond donors (a ‘canonical binding array’) complementary to the tet...
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Veröffentlicht in: | Chemistry & Biology 2001-06, Vol.8 (6), p.535-545 |
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description | The structures, obtained by X-ray crystallography, of the binding sites of catalytic antibodies raised to bind different phosphonates are compared. Although the amino acid sequences differ, all exhibit a tetrahedral array of hydrogen bond donors (a ‘canonical binding array’) complementary to the tetrahedral anion, which represents a ‘transition state epitope’ for the basic hydrolysis of esters and amides. Antibodies for phosphates, arsonates, and sulfonates are found also to possess the tetrahedral anion canonical binding array. |
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Antibodies for phosphates, arsonates, and sulfonates are found also to possess the tetrahedral anion canonical binding array.</description><subject>Animals</subject><subject>Anions</subject><subject>Antibodies - chemistry</subject><subject>Antibodies - immunology</subject><subject>Antibodies - metabolism</subject><subject>Antibody Specificity</subject><subject>Canonical binding array</subject><subject>Crystallography, X-Ray</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - metabolism</subject><subject>Esters</subject><subject>Haptens - immunology</subject><subject>Haptens - metabolism</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Immune system</subject><subject>Molecular recognition</subject><subject>Protein Conformation</subject><subject>Tetrahedral anion</subject><issn>1074-5521</issn><issn>1879-1301</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EoqXwCCCvECzS-o6TccwGoRE_lSp1Aawtx77pGCV28XWQ8hC8M57OIJZIlnwX3znXPoexlyAuQcD26isI1TZdt4E3At4KIWTXqEfsHHqlG5ACHtf5L3LGnhH9qBD0evuUnQG0IKSS5-z3zsYUg7MTH0L0Id5xm7NdiVvic5rQLZPNPKNLdzGUkCLHCWeMhXiIvOyRh3leInJaqeD8jhcs2e7R52ppYxVUq-gfSKxE5vvV5zStFIhXMtLRlYot-Jw9Ge1E-OJ0X7Dvnz5-231pbm4_X-8-3DSuE7I0vpWdUqqHjTtMIHstBuX0ph-Vd2OrlBic7rcS2rG1zqphVL32GrWs6XReXrDXR9_7nH4u9VlmDuRwmmzEtJBRQrewFW0FuyPociLKOJr7HGabVwPCHHowDz2YQ8hG1HPowaiqe3VasAwz-n-qU_AVeH8EsH7zV8BsyAWMDn2oWRfjU_jPij9Oy5pW</recordid><startdate>20010601</startdate><enddate>20010601</enddate><creator>Tantillo, Dean J</creator><creator>Houk, K.N</creator><general>Elsevier Ltd</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>20010601</creationdate><title>Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state</title><author>Tantillo, Dean J ; Houk, K.N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-d435777812c435713890b7c928f7dcf4770bc986314f4aca7bf789d9e938795d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Anions</topic><topic>Antibodies - chemistry</topic><topic>Antibodies - immunology</topic><topic>Antibodies - metabolism</topic><topic>Antibody Specificity</topic><topic>Canonical binding array</topic><topic>Crystallography, X-Ray</topic><topic>Epitopes - chemistry</topic><topic>Epitopes - metabolism</topic><topic>Esters</topic><topic>Haptens - immunology</topic><topic>Haptens - metabolism</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Immune system</topic><topic>Molecular recognition</topic><topic>Protein Conformation</topic><topic>Tetrahedral anion</topic><toplevel>online_resources</toplevel><creatorcontrib>Tantillo, Dean J</creatorcontrib><creatorcontrib>Houk, K.N</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Chemistry & Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tantillo, Dean J</au><au>Houk, K.N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state</atitle><jtitle>Chemistry & Biology</jtitle><addtitle>Chem Biol</addtitle><date>2001-06-01</date><risdate>2001</risdate><volume>8</volume><issue>6</issue><spage>535</spage><epage>545</epage><pages>535-545</pages><issn>1074-5521</issn><eissn>1879-1301</eissn><abstract>The structures, obtained by X-ray crystallography, of the binding sites of catalytic antibodies raised to bind different phosphonates are compared. 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subjects | Animals Anions Antibodies - chemistry Antibodies - immunology Antibodies - metabolism Antibody Specificity Canonical binding array Crystallography, X-Ray Epitopes - chemistry Epitopes - metabolism Esters Haptens - immunology Haptens - metabolism Humans Hydrolysis Immune system Molecular recognition Protein Conformation Tetrahedral anion |
title | Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state |
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