Crystal structure of dimeric HIV-1 capsid protein
X-ray diffraction analysis of a human immunodeficiency virus (HIV-1) capsid (CA) protein shows that each monomer within the dimer consists of seven α-helices, five of which are arranged in a coiled coil-like structure. Sequence assignments were made for two of the helices, and tentative connectivity...
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| Veröffentlicht in: | Nature Structural Biology 1996-09, Vol.3 (9), p.763-770 |
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| container_title | Nature Structural Biology |
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| creator | Momany, Cory Kovari, Ladislau C. Prongay, Andrew J. Keller, Walter Gitti, Rossitza K. Lee, Brian M. Gorbalenya, Alexander E. Tong, Liang McClure, Jan Ehrlich, Lorna S. Summers, Michael F. Carter, Carol Rossmann, Michael G. |
| description | X-ray diffraction analysis of a human immunodeficiency virus (HIV-1) capsid (CA) protein shows that each monomer within the dimer consists of seven α-helices, five of which are arranged in a coiled coil-like structure. Sequence assignments were made for two of the helices, and tentative connectivity of the remainder of the protein was confirmed by the recent solution structure of a monomeric N-terminal fragment. The C-terminal third of the protein is mostly disordered in the crystal. The longest helices in the coiled coil-like structure are separated by a long, highly antigenic peptide that includes the binding site of an antibody fragment complexed with CA in the crystal. The site of binding of the Fab, the position of the antigenic loop and the site of cleavage between the matrix protein and CA establish the side of the dimer that would be on the exterior of the retroviral core. |
| doi_str_mv | 10.1038/nsb0996-763 |
| format | Article |
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Sequence assignments were made for two of the helices, and tentative connectivity of the remainder of the protein was confirmed by the recent solution structure of a monomeric N-terminal fragment. The C-terminal third of the protein is mostly disordered in the crystal. The longest helices in the coiled coil-like structure are separated by a long, highly antigenic peptide that includes the binding site of an antibody fragment complexed with CA in the crystal. 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Sequence assignments were made for two of the helices, and tentative connectivity of the remainder of the protein was confirmed by the recent solution structure of a monomeric N-terminal fragment. The C-terminal third of the protein is mostly disordered in the crystal. The longest helices in the coiled coil-like structure are separated by a long, highly antigenic peptide that includes the binding site of an antibody fragment complexed with CA in the crystal. The site of binding of the Fab, the position of the antigenic loop and the site of cleavage between the matrix protein and CA establish the side of the dimer that would be on the exterior of the retroviral core.</description><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Binding Sites, Antibody</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Capsid - chemistry</subject><subject>Capsid - immunology</subject><subject>Conserved Sequence</subject><subject>Crystallography, X-Ray</subject><subject>HIV Antibodies - immunology</subject><subject>HIV-1 - chemistry</subject><subject>HIV-1 - immunology</subject><subject>human immunodeficiency virus 1</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Structure</subject><subject>Protein Structure, Secondary</subject><issn>1072-8368</issn><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEUhYMotVZXroVZudHoTTJ5LaWoLRTcqNswk0lkyjxqMrPov2-kgyvB1T1wPs6FD6FrAg8EmHrsYglaCywFO0FzwnOOtVb8NGWQFCsm1Dm6iHELQDmXbIZmSqqccZgjsgz7OBRNFocw2mEMLut9VtWtC7XNVutPTDJb7GJdZbvQD67uLtGZL5rorqa7QB8vz-_LFd68va6XTxtscwoDFloJEFo46SuqLPOS5r4kBTjBFC9AgWZEg2CcgwMtQJZKWWkJYUS50rMFuj3upr_fo4uDaetoXdMUnevHaKSimjAt_gUJl4JqkSfw7gja0McYnDe7ULdF2BsC5sekmUyaZDLRN9PsWLau-mUndam_P_YxNd2XC2bbj6FLSv6cOwAZqnpa</recordid><startdate>19960901</startdate><enddate>19960901</enddate><creator>Momany, Cory</creator><creator>Kovari, Ladislau C.</creator><creator>Prongay, Andrew J.</creator><creator>Keller, Walter</creator><creator>Gitti, Rossitza K.</creator><creator>Lee, Brian M.</creator><creator>Gorbalenya, Alexander E.</creator><creator>Tong, Liang</creator><creator>McClure, Jan</creator><creator>Ehrlich, Lorna S.</creator><creator>Summers, Michael F.</creator><creator>Carter, Carol</creator><creator>Rossmann, Michael G.</creator><general>Nature Publishing Group UK</general><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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19960901</creationdate><title>Crystal structure of dimeric HIV-1 capsid protein</title><author>Momany, Cory ; Kovari, Ladislau C. ; Prongay, Andrew J. ; Keller, Walter ; Gitti, Rossitza K. ; Lee, Brian M. ; Gorbalenya, Alexander E. ; Tong, Liang ; McClure, Jan ; Ehrlich, Lorna S. ; Summers, Michael F. ; Carter, Carol ; Rossmann, Michael G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-69860696e7fd28c3f724fb1a0e6385a0809319063550e09607b88c7c11318ebf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>AIDS/HIV</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Binding Sites, Antibody</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Capsid - chemistry</topic><topic>Capsid - immunology</topic><topic>Conserved Sequence</topic><topic>Crystallography, X-Ray</topic><topic>HIV Antibodies - immunology</topic><topic>HIV-1 - chemistry</topic><topic>HIV-1 - immunology</topic><topic>human immunodeficiency virus 1</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Protein Structure</topic><topic>Protein Structure, Secondary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Momany, Cory</creatorcontrib><creatorcontrib>Kovari, Ladislau C.</creatorcontrib><creatorcontrib>Prongay, Andrew J.</creatorcontrib><creatorcontrib>Keller, Walter</creatorcontrib><creatorcontrib>Gitti, Rossitza K.</creatorcontrib><creatorcontrib>Lee, Brian M.</creatorcontrib><creatorcontrib>Gorbalenya, Alexander E.</creatorcontrib><creatorcontrib>Tong, Liang</creatorcontrib><creatorcontrib>McClure, Jan</creatorcontrib><creatorcontrib>Ehrlich, Lorna S.</creatorcontrib><creatorcontrib>Summers, Michael F.</creatorcontrib><creatorcontrib>Carter, Carol</creatorcontrib><creatorcontrib>Rossmann, Michael G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Momany, Cory</au><au>Kovari, Ladislau C.</au><au>Prongay, Andrew J.</au><au>Keller, Walter</au><au>Gitti, Rossitza K.</au><au>Lee, Brian M.</au><au>Gorbalenya, Alexander E.</au><au>Tong, Liang</au><au>McClure, Jan</au><au>Ehrlich, Lorna S.</au><au>Summers, Michael F.</au><au>Carter, Carol</au><au>Rossmann, Michael G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of dimeric HIV-1 capsid protein</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>1996-09-01</date><risdate>1996</risdate><volume>3</volume><issue>9</issue><spage>763</spage><epage>770</epage><pages>763-770</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>X-ray diffraction analysis of a human immunodeficiency virus (HIV-1) capsid (CA) protein shows that each monomer within the dimer consists of seven α-helices, five of which are arranged in a coiled coil-like structure. Sequence assignments were made for two of the helices, and tentative connectivity of the remainder of the protein was confirmed by the recent solution structure of a monomeric N-terminal fragment. The C-terminal third of the protein is mostly disordered in the crystal. The longest helices in the coiled coil-like structure are separated by a long, highly antigenic peptide that includes the binding site of an antibody fragment complexed with CA in the crystal. The site of binding of the Fab, the position of the antigenic loop and the site of cleavage between the matrix protein and CA establish the side of the dimer that would be on the exterior of the retroviral core.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>8784350</pmid><doi>10.1038/nsb0996-763</doi><tpages>8</tpages></addata></record> |
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| ispartof | Nature Structural Biology, 1996-09, Vol.3 (9), p.763-770 |
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| language | eng |
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| subjects | AIDS/HIV Amino Acid Sequence Animals Antibodies, Monoclonal Binding Sites, Antibody Biochemistry Biological Microscopy Capsid - chemistry Capsid - immunology Conserved Sequence Crystallography, X-Ray HIV Antibodies - immunology HIV-1 - chemistry HIV-1 - immunology human immunodeficiency virus 1 Humans Life Sciences Membrane Biology Mice Molecular Sequence Data Protein Conformation Protein Structure Protein Structure, Secondary |
| title | Crystal structure of dimeric HIV-1 capsid protein |
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