Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition
The three-dimensional structure of a specific antibody (Fab 17/9) to a peptide immunogen from influenza virus hemagglutinin [HA1(75-110)] and two independent crystal complexes of this antibody with bound peptide (Tyr$^{P100}$-Leu$^{P108}$) have been determined by x-ray crystallographic techniques at...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1992-02, Vol.255 (5047), p.959-965 |
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| creator | Rini, James M. Schulze-Gahmen, Ursula Wilson, Ian A. |
| description | The three-dimensional structure of a specific antibody (Fab 17/9) to a peptide immunogen from influenza virus hemagglutinin [HA1(75-110)] and two independent crystal complexes of this antibody with bound peptide (Tyr$^{P100}$-Leu$^{P108}$) have been determined by x-ray crystallographic techniques at 2.0 $\angst $, 2.9 $\angst $, and 3.1 $\angst $ resolution, respectively. The nonapeptide antigen assumes a type I β turn in the antibody combining site and interacts primarily with the Fab hypervariable loops L3, H2, and H3. Comparison of the bound and unbound Fab structures shows that a major rearrangement in the H3 loop accompanies antigen binding. This conformational change results in the creation of a binding pocket for the β turn of the peptide, allowing Tyr$^{P105}$ to be accommodated. The conformation of the peptide bound to the antibody shows similarity to its cognate sequence in the HA1, suggesting a possible mechanism for the cross-reactivity of this Fab with monomeric hemagglutinin. The structures of the free and antigen bound antibodies demonstrate the flexibility of the antibody combining site and provide an example of induced fit as a mechanism for antibody-antigen recognition. |
| doi_str_mv | 10.1126/science.1546293 |
| format | Article |
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The nonapeptide antigen assumes a type I β turn in the antibody combining site and interacts primarily with the Fab hypervariable loops L3, H2, and H3. Comparison of the bound and unbound Fab structures shows that a major rearrangement in the H3 loop accompanies antigen binding. This conformational change results in the creation of a binding pocket for the β turn of the peptide, allowing Tyr$^{P105}$ to be accommodated. The conformation of the peptide bound to the antibody shows similarity to its cognate sequence in the HA1, suggesting a possible mechanism for the cross-reactivity of this Fab with monomeric hemagglutinin. The structures of the free and antigen bound antibodies demonstrate the flexibility of the antibody combining site and provide an example of induced fit as a mechanism for antibody-antigen recognition.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1546293</identifier><identifier>PMID: 1546293</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies ; Antibodies, immunoglobulins ; Antibodies, Monoclonal - ultrastructure ; Antigen-Antibody Reactions ; Antigens ; Atoms ; Binding sites ; Biological and medical sciences ; Biology ; Conformity ; Crystals ; Electron density ; Energy ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Hemagglutinins, Viral - immunology ; Hydrogen Bonding ; Hydrogen bonds ; Immune recognition ; Immunity (Disease) ; Immunoglobulin Fab Fragments - ultrastructure ; Immunoglobulin G - ultrastructure ; In Vitro Techniques ; Influenza A virus - immunology ; influenza virus ; Kinetics ; Mice ; Models, Molecular ; Molecular immunology ; Molecular Sequence Data ; Molecular structure ; Molecules ; Motion ; Peptides - chemistry ; Peptides - immunology ; Personality ; Protein Binding ; Protein Conformation ; Protein structure ; Proteins ; Research Article ; Structure ; Surface areas ; Thermodynamics ; Transcripts (Written Records) ; X-ray crystallography ; X-Ray Diffraction</subject><ispartof>Science (American Association for the Advancement of Science), 1992-02, Vol.255 (5047), p.959-965</ispartof><rights>Copyright 1992 American Association for the Advancement of Science</rights><rights>1992 INIST-CNRS</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Feb 21, 1992</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c772t-7e97fbd845a6e4f66fde7fa28cebf1263127c6fd80a08a2e22c726f07051c7893</citedby><cites>FETCH-LOGICAL-c772t-7e97fbd845a6e4f66fde7fa28cebf1263127c6fd80a08a2e22c726f07051c7893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2876584$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2876584$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5209961$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1546293$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rini, James M.</creatorcontrib><creatorcontrib>Schulze-Gahmen, Ursula</creatorcontrib><creatorcontrib>Wilson, Ian A.</creatorcontrib><title>Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The three-dimensional structure of a specific antibody (Fab 17/9) to a peptide immunogen from influenza virus hemagglutinin [HA1(75-110)] and two independent crystal complexes of this antibody with bound peptide (Tyr$^{P100}$-Leu$^{P108}$) have been determined by x-ray crystallographic techniques at 2.0 $\angst $, 2.9 $\angst $, and 3.1 $\angst $ resolution, respectively. The nonapeptide antigen assumes a type I β turn in the antibody combining site and interacts primarily with the Fab hypervariable loops L3, H2, and H3. Comparison of the bound and unbound Fab structures shows that a major rearrangement in the H3 loop accompanies antigen binding. This conformational change results in the creation of a binding pocket for the β turn of the peptide, allowing Tyr$^{P105}$ to be accommodated. The conformation of the peptide bound to the antibody shows similarity to its cognate sequence in the HA1, suggesting a possible mechanism for the cross-reactivity of this Fab with monomeric hemagglutinin. The structures of the free and antigen bound antibodies demonstrate the flexibility of the antibody combining site and provide an example of induced fit as a mechanism for antibody-antigen recognition.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, immunoglobulins</subject><subject>Antibodies, Monoclonal - ultrastructure</subject><subject>Antigen-Antibody Reactions</subject><subject>Antigens</subject><subject>Atoms</subject><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>Biology</subject><subject>Conformity</subject><subject>Crystals</subject><subject>Electron density</subject><subject>Energy</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Hemagglutinins, Viral - immunology</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Immune recognition</subject><subject>Immunity (Disease)</subject><subject>Immunoglobulin Fab Fragments - ultrastructure</subject><subject>Immunoglobulin G - ultrastructure</subject><subject>In Vitro Techniques</subject><subject>Influenza A virus - immunology</subject><subject>influenza virus</subject><subject>Kinetics</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular immunology</subject><subject>Molecular Sequence Data</subject><subject>Molecular structure</subject><subject>Molecules</subject><subject>Motion</subject><subject>Peptides - chemistry</subject><subject>Peptides - immunology</subject><subject>Personality</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Research Article</subject><subject>Structure</subject><subject>Surface areas</subject><subject>Thermodynamics</subject><subject>Transcripts (Written Records)</subject><subject>X-ray crystallography</subject><subject>X-Ray Diffraction</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0s9v0zAUB3ALgUZXOHMBKZoQcFg22_lh51iqrVQqVKLA1XKd5-IqtYedTOy_x6VRUVEFlQ-x3veTp9h5CL0g-IoQWl4HZcAquCJFXtIqe4QGBFdFWlGcPUYDjLMy5ZgVT9F5CGuMY1ZlZ-is5wO0WLS-U23nZZPc3Jt62yzRzidTW3cK6uTWtIkMiUw-gvourQmb3_HItmbp6od0u1mBTT6DcitrWuPsM_REyybA8_45RF9vb76MP6Sz-WQ6Hs1SxRhtUwYV08ua54UsIddlqWtgWlKuYKnj2TJCmYpFjiXmkgKlitFSY4YLohivsiF6u-t7592PDkIrNiYoaBppwXVBsDzLOc1jpyF6829J41dQRv8LSUlxxDjCi7_g2nXexuMKSrKiIJRnEV3u0Eo2IIzVrvVSxduCeN3OgjaxPCKkKjnLtz3TIzyuGjZGHfPvDnwkLfxsV7ILQUwXn06m828n0_eTUymfzA7o5TGqXNPACkSci_H8gF_vuPIuBA9a3Hmzkf5BECy2gy_6wRf9JMc3XvU_pFtuoP7j9_nrPpdByUZ7aZUJe1ZQXFUliezljq1D6_w-ppyVBc-zX9R-D0A</recordid><startdate>19920221</startdate><enddate>19920221</enddate><creator>Rini, James M.</creator><creator>Schulze-Gahmen, Ursula</creator><creator>Wilson, Ian A.</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>AEUYN</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>7T5</scope><scope>7X8</scope></search><sort><creationdate>19920221</creationdate><title>Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition</title><author>Rini, James M. ; Schulze-Gahmen, Ursula ; Wilson, Ian A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c772t-7e97fbd845a6e4f66fde7fa28cebf1263127c6fd80a08a2e22c726f07051c7893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, immunoglobulins</topic><topic>Antibodies, Monoclonal - ultrastructure</topic><topic>Antigen-Antibody Reactions</topic><topic>Antigens</topic><topic>Atoms</topic><topic>Binding sites</topic><topic>Biological and medical sciences</topic><topic>Biology</topic><topic>Conformity</topic><topic>Crystals</topic><topic>Electron density</topic><topic>Energy</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Hemagglutinins, Viral - immunology</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Immune recognition</topic><topic>Immunity (Disease)</topic><topic>Immunoglobulin Fab Fragments - ultrastructure</topic><topic>Immunoglobulin G - ultrastructure</topic><topic>In Vitro Techniques</topic><topic>Influenza A virus - immunology</topic><topic>influenza virus</topic><topic>Kinetics</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Molecular immunology</topic><topic>Molecular Sequence Data</topic><topic>Molecular structure</topic><topic>Molecules</topic><topic>Motion</topic><topic>Peptides - chemistry</topic><topic>Peptides - immunology</topic><topic>Personality</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Research Article</topic><topic>Structure</topic><topic>Surface 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Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rini, James M.</au><au>Schulze-Gahmen, Ursula</au><au>Wilson, Ian A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1992-02-21</date><risdate>1992</risdate><volume>255</volume><issue>5047</issue><spage>959</spage><epage>965</epage><pages>959-965</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The three-dimensional structure of a specific antibody (Fab 17/9) to a peptide immunogen from influenza virus hemagglutinin [HA1(75-110)] and two independent crystal complexes of this antibody with bound peptide (Tyr$^{P100}$-Leu$^{P108}$) have been determined by x-ray crystallographic techniques at 2.0 $\angst $, 2.9 $\angst $, and 3.1 $\angst $ resolution, respectively. The nonapeptide antigen assumes a type I β turn in the antibody combining site and interacts primarily with the Fab hypervariable loops L3, H2, and H3. Comparison of the bound and unbound Fab structures shows that a major rearrangement in the H3 loop accompanies antigen binding. This conformational change results in the creation of a binding pocket for the β turn of the peptide, allowing Tyr$^{P105}$ to be accommodated. The conformation of the peptide bound to the antibody shows similarity to its cognate sequence in the HA1, suggesting a possible mechanism for the cross-reactivity of this Fab with monomeric hemagglutinin. The structures of the free and antigen bound antibodies demonstrate the flexibility of the antibody combining site and provide an example of induced fit as a mechanism for antibody-antigen recognition.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>1546293</pmid><doi>10.1126/science.1546293</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1992-02, Vol.255 (5047), p.959-965 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743482426 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Amino Acid Sequence Animals Antibodies Antibodies, immunoglobulins Antibodies, Monoclonal - ultrastructure Antigen-Antibody Reactions Antigens Atoms Binding sites Biological and medical sciences Biology Conformity Crystals Electron density Energy Fundamental and applied biological sciences. Psychology Fundamental immunology Hemagglutinins, Viral - immunology Hydrogen Bonding Hydrogen bonds Immune recognition Immunity (Disease) Immunoglobulin Fab Fragments - ultrastructure Immunoglobulin G - ultrastructure In Vitro Techniques Influenza A virus - immunology influenza virus Kinetics Mice Models, Molecular Molecular immunology Molecular Sequence Data Molecular structure Molecules Motion Peptides - chemistry Peptides - immunology Personality Protein Binding Protein Conformation Protein structure Proteins Research Article Structure Surface areas Thermodynamics Transcripts (Written Records) X-ray crystallography X-Ray Diffraction |
| title | Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition |
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