Refined structures of Bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment
The HyHEL‐5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg‐white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has b...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1996-09, Vol.26 (1), p.55-65 |
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| creator | Chacko, Susan Silverton, Enid W. Smith-Gill, Sandra J. Davies, David R. Shick, Kari A. Xavier, K. Asish Willson, Richard C. Jeffrey, Philip D. Chang, Chieh Ying Y. Sieker, Larry C. Sheriff, Steven |
| description | The HyHEL‐5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg‐white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has been determined in the uncomplexed state in two different crystal forms and in the complexed state with HyHEL‐5, an anti‐hen egg‐white lysozyme Fab. Similar backbone conformations are observed in the three molecules of the two crystal forms of uncomplexed BWQL, although they show considerable variability in side‐chain conformation. A relatively mobile segment in uncomplexed BWQL is observed to be part of the HyHEL‐5 epitope. No major backbone conformational differences are observed in the lysozyme upon complex formation, but side‐chain conformational differences are seen in surface residues that are involved in the interface with the antibody. The hydrogen bonding in the interface between BWQL and HyHEL‐5 is similar to that in previously determined lysozyme‐HyHEL‐5 complexes. © 1996 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/(SICI)1097-0134(199609)26:1<55::AID-PROT5>3.0.CO;2-F |
| format | Article |
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Asish ; Willson, Richard C. ; Jeffrey, Philip D. ; Chang, Chieh Ying Y. ; Sieker, Larry C. ; Sheriff, Steven</creator><creatorcontrib>Chacko, Susan ; Silverton, Enid W. ; Smith-Gill, Sandra J. ; Davies, David R. ; Shick, Kari A. ; Xavier, K. Asish ; Willson, Richard C. ; Jeffrey, Philip D. ; Chang, Chieh Ying Y. ; Sieker, Larry C. ; Sheriff, Steven</creatorcontrib><description>The HyHEL‐5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg‐white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has been determined in the uncomplexed state in two different crystal forms and in the complexed state with HyHEL‐5, an anti‐hen egg‐white lysozyme Fab. Similar backbone conformations are observed in the three molecules of the two crystal forms of uncomplexed BWQL, although they show considerable variability in side‐chain conformation. A relatively mobile segment in uncomplexed BWQL is observed to be part of the HyHEL‐5 epitope. No major backbone conformational differences are observed in the lysozyme upon complex formation, but side‐chain conformational differences are seen in surface residues that are involved in the interface with the antibody. The hydrogen bonding in the interface between BWQL and HyHEL‐5 is similar to that in previously determined lysozyme‐HyHEL‐5 complexes. © 1996 Wiley‐Liss, Inc.</description><identifier>ISSN: 0887-3585</identifier><identifier>EISSN: 1097-0134</identifier><identifier>DOI: 10.1002/(SICI)1097-0134(199609)26:1<55::AID-PROT5>3.0.CO;2-F</identifier><identifier>PMID: 8880929</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; anti-protein Fab ; antibody-antigen complex ; Antigen-Antibody Complex - chemistry ; avian lysozyme ; Chickens ; Crystallization ; Crystallography, X-Ray ; Egg Proteins - chemistry ; Epitope Mapping ; Hydrogen Bonding ; Immunoglobulin Fab Fragments - chemistry ; Immunoglobulin Fab Fragments - immunology ; Immunoglobulin Fab Fragments - metabolism ; Models, Molecular ; Muramidase - chemistry ; Muramidase - immunology ; Muramidase - metabolism ; Mutation - genetics ; Protein Conformation ; Quail ; Water - metabolism</subject><ispartof>Proteins, structure, function, and bioinformatics, 1996-09, Vol.26 (1), p.55-65</ispartof><rights>Copyright © 1996 Wiley‐Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4015-b34013ca92d42572b54325e0b8515959a8db53f6d2f07c42e27c2eadb35f6523</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F%28SICI%291097-0134%28199609%2926%3A1%3C55%3A%3AAID-PROT5%3E3.0.CO%3B2-F$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F%28SICI%291097-0134%28199609%2926%3A1%3C55%3A%3AAID-PROT5%3E3.0.CO%3B2-F$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8880929$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chacko, Susan</creatorcontrib><creatorcontrib>Silverton, Enid W.</creatorcontrib><creatorcontrib>Smith-Gill, Sandra J.</creatorcontrib><creatorcontrib>Davies, David R.</creatorcontrib><creatorcontrib>Shick, Kari A.</creatorcontrib><creatorcontrib>Xavier, K. Asish</creatorcontrib><creatorcontrib>Willson, Richard C.</creatorcontrib><creatorcontrib>Jeffrey, Philip D.</creatorcontrib><creatorcontrib>Chang, Chieh Ying Y.</creatorcontrib><creatorcontrib>Sieker, Larry C.</creatorcontrib><creatorcontrib>Sheriff, Steven</creatorcontrib><title>Refined structures of Bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment</title><title>Proteins, structure, function, and bioinformatics</title><addtitle>Proteins</addtitle><description>The HyHEL‐5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg‐white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has been determined in the uncomplexed state in two different crystal forms and in the complexed state with HyHEL‐5, an anti‐hen egg‐white lysozyme Fab. Similar backbone conformations are observed in the three molecules of the two crystal forms of uncomplexed BWQL, although they show considerable variability in side‐chain conformation. A relatively mobile segment in uncomplexed BWQL is observed to be part of the HyHEL‐5 epitope. No major backbone conformational differences are observed in the lysozyme upon complex formation, but side‐chain conformational differences are seen in surface residues that are involved in the interface with the antibody. The hydrogen bonding in the interface between BWQL and HyHEL‐5 is similar to that in previously determined lysozyme‐HyHEL‐5 complexes. © 1996 Wiley‐Liss, Inc.</description><subject>Animals</subject><subject>anti-protein Fab</subject><subject>antibody-antigen complex</subject><subject>Antigen-Antibody Complex - chemistry</subject><subject>avian lysozyme</subject><subject>Chickens</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Egg Proteins - chemistry</subject><subject>Epitope Mapping</subject><subject>Hydrogen Bonding</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin Fab Fragments - immunology</subject><subject>Immunoglobulin Fab Fragments - metabolism</subject><subject>Models, Molecular</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - immunology</subject><subject>Muramidase - metabolism</subject><subject>Mutation - genetics</subject><subject>Protein Conformation</subject><subject>Quail</subject><subject>Water - metabolism</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v00AQQFcIVELhJ1TaE2oPDvvhtb2hQipu0wRFTdWmQuIyWttjYvBH6rWVml-Pg6NwAPU02h3Ne9Ij5JyzMWdMfDi9n4fzM8607zAu3VOutcf0mfAm_FypyeRifunc3i1X6pMcs3G4_Cic6QsyOhy8JCMWBL4jVaBekzfW_mCMeVp6R-QoCAKmhR4RvMM0KzGhtqnbuGlrtLRK6ecq2q6zBulja7Kc5p2tfnUF0raMq2KT41N_YcqE_n1ts2ZNmzXSWTe7WjiKTk1E09p8L7Bs3pJXqcktvtvPY7KaXq3CmbNYXs_Di4UTu4wrJ5L9kLHRInGF8kWkXCkUsihQXGmlTZBESqZeIlLmx65A4ccCTRJJlXpKyGPyfsBu6uqxRdtAkdkY89yUWLUW_MD1pBS-PPjjurK2xhQ2dVaYugPOYBcfYBcfdi1h1xKG-CA84KAUQB8f_sQHCQzCJQiY9tiTvb-NCkwO0H3tfv8w7LdZjt0_zueV_zMOHz3XGbiZbfDpwDX1T_B86Sv4enMNt5fu_ZfwmwQhfwOizq6_</recordid><startdate>199609</startdate><enddate>199609</enddate><creator>Chacko, Susan</creator><creator>Silverton, Enid W.</creator><creator>Smith-Gill, Sandra J.</creator><creator>Davies, David R.</creator><creator>Shick, Kari A.</creator><creator>Xavier, K. Asish</creator><creator>Willson, Richard C.</creator><creator>Jeffrey, Philip D.</creator><creator>Chang, Chieh Ying Y.</creator><creator>Sieker, Larry C.</creator><creator>Sheriff, Steven</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</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>199609</creationdate><title>Refined structures of Bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment</title><author>Chacko, Susan ; Silverton, Enid W. ; Smith-Gill, Sandra J. ; Davies, David R. ; Shick, Kari A. ; Xavier, K. Asish ; Willson, Richard C. ; Jeffrey, Philip D. ; Chang, Chieh Ying Y. ; Sieker, Larry C. ; Sheriff, Steven</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4015-b34013ca92d42572b54325e0b8515959a8db53f6d2f07c42e27c2eadb35f6523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>anti-protein Fab</topic><topic>antibody-antigen complex</topic><topic>Antigen-Antibody Complex - chemistry</topic><topic>avian lysozyme</topic><topic>Chickens</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Egg Proteins - chemistry</topic><topic>Epitope Mapping</topic><topic>Hydrogen Bonding</topic><topic>Immunoglobulin Fab Fragments - chemistry</topic><topic>Immunoglobulin Fab Fragments - immunology</topic><topic>Immunoglobulin Fab Fragments - metabolism</topic><topic>Models, Molecular</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - immunology</topic><topic>Muramidase - metabolism</topic><topic>Mutation - genetics</topic><topic>Protein Conformation</topic><topic>Quail</topic><topic>Water - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chacko, Susan</creatorcontrib><creatorcontrib>Silverton, Enid W.</creatorcontrib><creatorcontrib>Smith-Gill, Sandra J.</creatorcontrib><creatorcontrib>Davies, David R.</creatorcontrib><creatorcontrib>Shick, Kari A.</creatorcontrib><creatorcontrib>Xavier, K. Asish</creatorcontrib><creatorcontrib>Willson, Richard C.</creatorcontrib><creatorcontrib>Jeffrey, Philip D.</creatorcontrib><creatorcontrib>Chang, Chieh Ying Y.</creatorcontrib><creatorcontrib>Sieker, Larry C.</creatorcontrib><creatorcontrib>Sheriff, Steven</creatorcontrib><collection>Istex</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>Proteins, structure, function, and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chacko, Susan</au><au>Silverton, Enid W.</au><au>Smith-Gill, Sandra J.</au><au>Davies, David R.</au><au>Shick, Kari A.</au><au>Xavier, K. Asish</au><au>Willson, Richard C.</au><au>Jeffrey, Philip D.</au><au>Chang, Chieh Ying Y.</au><au>Sieker, Larry C.</au><au>Sheriff, Steven</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Refined structures of Bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>1996-09</date><risdate>1996</risdate><volume>26</volume><issue>1</issue><spage>55</spage><epage>65</epage><pages>55-65</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>The HyHEL‐5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg‐white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has been determined in the uncomplexed state in two different crystal forms and in the complexed state with HyHEL‐5, an anti‐hen egg‐white lysozyme Fab. Similar backbone conformations are observed in the three molecules of the two crystal forms of uncomplexed BWQL, although they show considerable variability in side‐chain conformation. A relatively mobile segment in uncomplexed BWQL is observed to be part of the HyHEL‐5 epitope. No major backbone conformational differences are observed in the lysozyme upon complex formation, but side‐chain conformational differences are seen in surface residues that are involved in the interface with the antibody. The hydrogen bonding in the interface between BWQL and HyHEL‐5 is similar to that in previously determined lysozyme‐HyHEL‐5 complexes. © 1996 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>8880929</pmid><doi>10.1002/(SICI)1097-0134(199609)26:1<55::AID-PROT5>3.0.CO;2-F</doi><tpages>11</tpages></addata></record> |
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| identifier | ISSN: 0887-3585 |
| ispartof | Proteins, structure, function, and bioinformatics, 1996-09, Vol.26 (1), p.55-65 |
| issn | 0887-3585 1097-0134 |
| language | eng |
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| source | MEDLINE; Access via Wiley Online Library |
| subjects | Animals anti-protein Fab antibody-antigen complex Antigen-Antibody Complex - chemistry avian lysozyme Chickens Crystallization Crystallography, X-Ray Egg Proteins - chemistry Epitope Mapping Hydrogen Bonding Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - immunology Immunoglobulin Fab Fragments - metabolism Models, Molecular Muramidase - chemistry Muramidase - immunology Muramidase - metabolism Mutation - genetics Protein Conformation Quail Water - metabolism |
| title | Refined structures of Bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment |
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