The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition
BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 Å resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR...
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| Veröffentlicht in: | Biochemistry (Easton) 2006-10, Vol.45 (43), p.12917-12928 |
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| container_issue | 43 |
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| container_title | Biochemistry (Easton) |
| container_volume | 45 |
| creator | Casal, Eva Federici, Luca Zhang, Wei Fernandez-Recio, Juan Priego, Eva-Maria Miguel, Ricardo Nuñez DuHadaway, James B Prendergast, George C Luisi, Ben F Laue, Ernest D |
| description | BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 Å resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon “knobs-into-holes” packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein−protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups may differ in their potential to form regulatory heterotypic interactions. |
| doi_str_mv | 10.1021/bi060717k |
| format | Article |
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Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 Å resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon “knobs-into-holes” packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein−protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups may differ in their potential to form regulatory heterotypic interactions.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi060717k</identifier><identifier>PMID: 17059209</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Adaptor Proteins, Signal Transducing - chemistry ; Adaptor Proteins, Signal Transducing - metabolism ; Animals ; Binding Sites ; Crystallization ; Crystallography, X-Ray - methods ; Humans ; Models, Molecular ; Nuclear Proteins - chemistry ; Nuclear Proteins - metabolism ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Structural Homology, Protein ; Tumor Suppressor Proteins - chemistry ; Tumor Suppressor Proteins - metabolism</subject><ispartof>Biochemistry (Easton), 2006-10, Vol.45 (43), p.12917-12928</ispartof><rights>Copyright © 2006 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a507t-68f3196725d1f3341bbbffe4198afe53fce258b9e31364d3031c325b0800858c3</citedby><cites>FETCH-LOGICAL-a507t-68f3196725d1f3341bbbffe4198afe53fce258b9e31364d3031c325b0800858c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi060717k$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi060717k$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17059209$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Casal, Eva</creatorcontrib><creatorcontrib>Federici, Luca</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><creatorcontrib>Fernandez-Recio, Juan</creatorcontrib><creatorcontrib>Priego, Eva-Maria</creatorcontrib><creatorcontrib>Miguel, Ricardo Nuñez</creatorcontrib><creatorcontrib>DuHadaway, James B</creatorcontrib><creatorcontrib>Prendergast, George C</creatorcontrib><creatorcontrib>Luisi, Ben F</creatorcontrib><creatorcontrib>Laue, Ernest D</creatorcontrib><title>The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 Å resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon “knobs-into-holes” packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein−protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups may differ in their potential to form regulatory heterotypic interactions.</description><subject>Adaptor Proteins, Signal Transducing - chemistry</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray - methods</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Structural Homology, Protein</subject><subject>Tumor Suppressor Proteins - chemistry</subject><subject>Tumor Suppressor Proteins - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkV1v0zAUhiMEYt3ggj-AfAMSF2HHdhzHN0hdGVvE-OoKXFqOa6_ekjjYDqL_nkytCkhcHVnPo_cc-c2yZxheYyD4tHFQAsf87kE2w4xAXgjBHmYzAChzIko4yo5jvJ2eBfDicXaEOTBBQMyycbUxaBG2MakWXacw6jQGg7xFaQJn8yV66zvlemSD79Dl2Kkenbken867YeOGzTZOrK6R6teoThHV3dA6rZLzfUTWB_TBt0aPrQpoabS_6d09epI9sqqN5ul-nmRf352vFpf51aeLejG_yhUDnvKyshSLkhO2xpbSAjdNY60psKiUNYxabQirGmEopmWxpkCxpoQ1UAFUrNL0JHuzyx3GpjNrbfoUVCuH4DoVttIrJ_8lvdvIG_9TEsYJ8GoKeLkPCP7HaGKSnYvatK3qjR-jLCshADiZxFc7UQcfYzD2sASDvC9JHkqa3Od_X_XH3LcyCflOcDGZXweuwp0sOeVMrj5fy4vll_fw8ftSfpv8Fztf6Shv_Rj66VP_s_g3Of2oxw</recordid><startdate>20061031</startdate><enddate>20061031</enddate><creator>Casal, Eva</creator><creator>Federici, Luca</creator><creator>Zhang, Wei</creator><creator>Fernandez-Recio, Juan</creator><creator>Priego, Eva-Maria</creator><creator>Miguel, Ricardo Nuñez</creator><creator>DuHadaway, James B</creator><creator>Prendergast, George C</creator><creator>Luisi, Ben F</creator><creator>Laue, Ernest D</creator><general>American Chemical Society</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><scope>5PM</scope></search><sort><creationdate>20061031</creationdate><title>The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition</title><author>Casal, Eva ; Federici, Luca ; Zhang, Wei ; Fernandez-Recio, Juan ; Priego, Eva-Maria ; Miguel, Ricardo Nuñez ; DuHadaway, James B ; Prendergast, George C ; Luisi, Ben F ; Laue, Ernest D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a507t-68f3196725d1f3341bbbffe4198afe53fce258b9e31364d3031c325b0800858c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adaptor Proteins, Signal Transducing - chemistry</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray - methods</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Structural Homology, Protein</topic><topic>Tumor Suppressor Proteins - chemistry</topic><topic>Tumor Suppressor Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Casal, Eva</creatorcontrib><creatorcontrib>Federici, Luca</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><creatorcontrib>Fernandez-Recio, Juan</creatorcontrib><creatorcontrib>Priego, Eva-Maria</creatorcontrib><creatorcontrib>Miguel, Ricardo Nuñez</creatorcontrib><creatorcontrib>DuHadaway, James B</creatorcontrib><creatorcontrib>Prendergast, George C</creatorcontrib><creatorcontrib>Luisi, Ben F</creatorcontrib><creatorcontrib>Laue, Ernest D</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Casal, Eva</au><au>Federici, Luca</au><au>Zhang, Wei</au><au>Fernandez-Recio, Juan</au><au>Priego, Eva-Maria</au><au>Miguel, Ricardo Nuñez</au><au>DuHadaway, James B</au><au>Prendergast, George C</au><au>Luisi, Ben F</au><au>Laue, Ernest D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2006-10-31</date><risdate>2006</risdate><volume>45</volume><issue>43</issue><spage>12917</spage><epage>12928</epage><pages>12917-12928</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 Å resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon “knobs-into-holes” packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein−protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. 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| ispartof | Biochemistry (Easton), 2006-10, Vol.45 (43), p.12917-12928 |
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| subjects | Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - metabolism Animals Binding Sites Crystallization Crystallography, X-Ray - methods Humans Models, Molecular Nuclear Proteins - chemistry Nuclear Proteins - metabolism Protein Binding Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary Structural Homology, Protein Tumor Suppressor Proteins - chemistry Tumor Suppressor Proteins - metabolism |
| title | The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition |
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