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Probing the molecular basis of allergy. Three-dimensional structure of the bovine lipocalin allergen Bos d 2
The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-A resolution. Structurally Bos d 2 is a member of the lipocalin family comprising proteins with transport functions. There is a flat small cavity inside the Bos d 2 protein core...
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| Published in: | The Journal of biological chemistry 1999-01, Vol.274 (4), p.2337-2343 |
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| Main Authors: | , , , , , , |
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| Language: | English |
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| container_end_page | 2343 |
| container_issue | 4 |
| container_start_page | 2337 |
| container_title | The Journal of biological chemistry |
| container_volume | 274 |
| creator | Rouvinen, J. (University of Joensuu, Joensuu, Finland.) Rautiainen, J Virtanen, T Zeiler, T Kauppinen, J Taivainen, A Mantyjarvi, R |
| description | The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-A resolution. Structurally Bos d 2 is a member of the lipocalin family comprising proteins with transport functions. There is a flat small cavity inside the Bos d 2 protein core suitable for ligand binding, and it is possible that Glu115 and Asn37 inside the core are able to make hydrogen bonds with the ligand. Many allergens from different animals belong to the lipocalin family. The amino acid residue similarities between these lipocalins indicate putative regions for IgE binding. Comparison with the available allergen structures from other sources suggests that these allergens are roughly the same size and that their shape is more spherical than elliptical. |
| doi_str_mv | 10.1074/jbc.274.4.2337 |
| format | article |
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The amino acid residue similarities between these lipocalins indicate putative regions for IgE binding. Comparison with the available allergen structures from other sources suggests that these allergens are roughly the same size and that their shape is more spherical than elliptical.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.4.2337</identifier><identifier>PMID: 9891000</identifier><language>eng</language><publisher>United States</publisher><subject>ALERGENOS ; ALLERGENE ; ALLERGENS ; Allergens - chemistry ; Allergens - immunology ; Amino Acid Sequence ; ANALYTICAL METHODS ; ANIMAL PROTEINS ; Animals ; ANTIGENE ; ANTIGENOS ; ANTIGENS ; Antigens, Plant ; BINDING SITES ; BOVIN ; Carrier Proteins - chemistry ; Carrier Proteins - immunology ; CATTLE ; Crystallography, X-Ray ; EPITOPES ; GANADO BOVINO ; GENERO HUMANO ; GENRE HUMAIN ; IGE ; IMMUNOGLOBULINE ; IMMUNOGLOBULINS ; INMUNOGLOBULINA ; MANKIND ; MOLECULAR CONFORMATION ; Molecular Probes ; Molecular Sequence Data ; PDB/1BJ7 ; Protein Conformation ; PROTEINAS ; PROTEINE ; PROTEINS ; Recombinant Proteins - chemistry ; Recombinant Proteins - immunology ; Sequence Homology, Amino Acid ; TECHNIQUE ANALYTIQUE ; TECNICAS ANALITICAS ; X RAY DIFFRACTION</subject><ispartof>The Journal of biological chemistry, 1999-01, Vol.274 (4), p.2337-2343</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9891000$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rouvinen, J. (University of Joensuu, Joensuu, Finland.)</creatorcontrib><creatorcontrib>Rautiainen, J</creatorcontrib><creatorcontrib>Virtanen, T</creatorcontrib><creatorcontrib>Zeiler, T</creatorcontrib><creatorcontrib>Kauppinen, J</creatorcontrib><creatorcontrib>Taivainen, A</creatorcontrib><creatorcontrib>Mantyjarvi, R</creatorcontrib><title>Probing the molecular basis of allergy. Three-dimensional structure of the bovine lipocalin allergen Bos d 2</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-A resolution. Structurally Bos d 2 is a member of the lipocalin family comprising proteins with transport functions. There is a flat small cavity inside the Bos d 2 protein core suitable for ligand binding, and it is possible that Glu115 and Asn37 inside the core are able to make hydrogen bonds with the ligand. Many allergens from different animals belong to the lipocalin family. The amino acid residue similarities between these lipocalins indicate putative regions for IgE binding. Comparison with the available allergen structures from other sources suggests that these allergens are roughly the same size and that their shape is more spherical than elliptical.</description><subject>ALERGENOS</subject><subject>ALLERGENE</subject><subject>ALLERGENS</subject><subject>Allergens - chemistry</subject><subject>Allergens - immunology</subject><subject>Amino Acid Sequence</subject><subject>ANALYTICAL METHODS</subject><subject>ANIMAL PROTEINS</subject><subject>Animals</subject><subject>ANTIGENE</subject><subject>ANTIGENOS</subject><subject>ANTIGENS</subject><subject>Antigens, Plant</subject><subject>BINDING SITES</subject><subject>BOVIN</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - immunology</subject><subject>CATTLE</subject><subject>Crystallography, X-Ray</subject><subject>EPITOPES</subject><subject>GANADO BOVINO</subject><subject>GENERO HUMANO</subject><subject>GENRE HUMAIN</subject><subject>IGE</subject><subject>IMMUNOGLOBULINE</subject><subject>IMMUNOGLOBULINS</subject><subject>INMUNOGLOBULINA</subject><subject>MANKIND</subject><subject>MOLECULAR CONFORMATION</subject><subject>Molecular Probes</subject><subject>Molecular Sequence Data</subject><subject>PDB/1BJ7</subject><subject>Protein Conformation</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - immunology</subject><subject>Sequence Homology, Amino Acid</subject><subject>TECHNIQUE ANALYTIQUE</subject><subject>TECNICAS ANALITICAS</subject><subject>X RAY DIFFRACTION</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNpFkM1LxDAQxYMo67p69Sbk5K01H02aHFX8ggUFd8FbSdrpbiRt1qQV9r-34oJzeTPM7z2YQeiSkpySsrj5tHXOyiIvcsZ5eYTmlCiecUE_jtGcEEYzzYQ6RWcpfZKpCk1naKaVptMwR_4tBuv6DR62gLvgoR69idia5BIOLTbeQ9zsc7zaRoCscR30yYXeeJyGONbDGOGX-7Xb8O16wN7tQm286w9m6PFdSLjB7BydtMYnuDjoAq0fH1b3z9ny9enl_naZtYypIWtJAVYIqpSxTJZCFA3TQtemaWRp-NS2WjacylYAV5I0yohSgrWyMDWfzl-g67_cXQxfI6Sh6lyqwXvTQxhTJbWQhJZ8Aq8O4Gg7aKpddJ2J--rwnv99a0JlNtGlav1OtdaEaK5K_gNEWHBK</recordid><startdate>19990122</startdate><enddate>19990122</enddate><creator>Rouvinen, J. 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(University of Joensuu, Joensuu, Finland.) ; Rautiainen, J ; Virtanen, T ; Zeiler, T ; Kauppinen, J ; Taivainen, A ; Mantyjarvi, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f228t-f04eb55188ab267554d2959cadd67a3959f96d316f5e3860d8a576ebb64ac3083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>ALERGENOS</topic><topic>ALLERGENE</topic><topic>ALLERGENS</topic><topic>Allergens - chemistry</topic><topic>Allergens - immunology</topic><topic>Amino Acid Sequence</topic><topic>ANALYTICAL METHODS</topic><topic>ANIMAL PROTEINS</topic><topic>Animals</topic><topic>ANTIGENE</topic><topic>ANTIGENOS</topic><topic>ANTIGENS</topic><topic>Antigens, Plant</topic><topic>BINDING SITES</topic><topic>BOVIN</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - immunology</topic><topic>CATTLE</topic><topic>Crystallography, X-Ray</topic><topic>EPITOPES</topic><topic>GANADO BOVINO</topic><topic>GENERO HUMANO</topic><topic>GENRE HUMAIN</topic><topic>IGE</topic><topic>IMMUNOGLOBULINE</topic><topic>IMMUNOGLOBULINS</topic><topic>INMUNOGLOBULINA</topic><topic>MANKIND</topic><topic>MOLECULAR CONFORMATION</topic><topic>Molecular Probes</topic><topic>Molecular Sequence Data</topic><topic>PDB/1BJ7</topic><topic>Protein Conformation</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - immunology</topic><topic>Sequence Homology, Amino Acid</topic><topic>TECHNIQUE ANALYTIQUE</topic><topic>TECNICAS ANALITICAS</topic><topic>X RAY DIFFRACTION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rouvinen, J. (University of Joensuu, Joensuu, Finland.)</creatorcontrib><creatorcontrib>Rautiainen, J</creatorcontrib><creatorcontrib>Virtanen, T</creatorcontrib><creatorcontrib>Zeiler, T</creatorcontrib><creatorcontrib>Kauppinen, J</creatorcontrib><creatorcontrib>Taivainen, A</creatorcontrib><creatorcontrib>Mantyjarvi, R</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rouvinen, J. (University of Joensuu, Joensuu, Finland.)</au><au>Rautiainen, J</au><au>Virtanen, T</au><au>Zeiler, T</au><au>Kauppinen, J</au><au>Taivainen, A</au><au>Mantyjarvi, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Probing the molecular basis of allergy. Three-dimensional structure of the bovine lipocalin allergen Bos d 2</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-01-22</date><risdate>1999</risdate><volume>274</volume><issue>4</issue><spage>2337</spage><epage>2343</epage><pages>2337-2343</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-A resolution. Structurally Bos d 2 is a member of the lipocalin family comprising proteins with transport functions. There is a flat small cavity inside the Bos d 2 protein core suitable for ligand binding, and it is possible that Glu115 and Asn37 inside the core are able to make hydrogen bonds with the ligand. Many allergens from different animals belong to the lipocalin family. The amino acid residue similarities between these lipocalins indicate putative regions for IgE binding. Comparison with the available allergen structures from other sources suggests that these allergens are roughly the same size and that their shape is more spherical than elliptical.</abstract><cop>United States</cop><pmid>9891000</pmid><doi>10.1074/jbc.274.4.2337</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1999-01, Vol.274 (4), p.2337-2343 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | ScienceDirect Journals |
| subjects | ALERGENOS ALLERGENE ALLERGENS Allergens - chemistry Allergens - immunology Amino Acid Sequence ANALYTICAL METHODS ANIMAL PROTEINS Animals ANTIGENE ANTIGENOS ANTIGENS Antigens, Plant BINDING SITES BOVIN Carrier Proteins - chemistry Carrier Proteins - immunology CATTLE Crystallography, X-Ray EPITOPES GANADO BOVINO GENERO HUMANO GENRE HUMAIN IGE IMMUNOGLOBULINE IMMUNOGLOBULINS INMUNOGLOBULINA MANKIND MOLECULAR CONFORMATION Molecular Probes Molecular Sequence Data PDB/1BJ7 Protein Conformation PROTEINAS PROTEINE PROTEINS Recombinant Proteins - chemistry Recombinant Proteins - immunology Sequence Homology, Amino Acid TECHNIQUE ANALYTIQUE TECNICAS ANALITICAS X RAY DIFFRACTION |
| title | Probing the molecular basis of allergy. Three-dimensional structure of the bovine lipocalin allergen Bos d 2 |
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