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Fibronectin type III domains engineered to bind CD40L: cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of two complexes
Tn3 proteins are a novel class of binding molecules based on the third fibronectin type III domain of human tenascin C. Target‐specific Tn3 proteins are selected from combinatorial libraries in which three surface‐exposed loops have been diversified. Here, the cocrystallization of two different Tn3...
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| Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2013-09, Vol.69 (9), p.1045-1048 |
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| cites | cdi_FETCH-LOGICAL-c5482-51a3511c5c78f5e495e599f0bb53ed20b9e0869e46e0c43293363a6358ba69313 |
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| container_issue | 9 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Oganesyan, Vaheh Ferguson, Andrew Grinberg, Luba Wang, Lin Phipps, Sandrina Chacko, Benoy Drabic, Stacey Thisted, Thomas Baca, Manuel |
| description | Tn3 proteins are a novel class of binding molecules based on the third fibronectin type III domain of human tenascin C. Target‐specific Tn3 proteins are selected from combinatorial libraries in which three surface‐exposed loops have been diversified. Here, the cocrystallization of two different Tn3 proteins in complex with CD40L, a therapeutic target for immunological disease, is reported. These crystal structures are the first to be reported of Tn3 proteins and will help to reveal how these engineered molecules achieve specific recognition of a cognate target. |
| doi_str_mv | 10.1107/S1744309113022847 |
| format | article |
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Target‐specific Tn3 proteins are selected from combinatorial libraries in which three surface‐exposed loops have been diversified. Here, the cocrystallization of two different Tn3 proteins in complex with CD40L, a therapeutic target for immunological disease, is reported. These crystal structures are the first to be reported of Tn3 proteins and will help to reveal how these engineered molecules achieve specific recognition of a cognate target.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S1744309113022847</identifier><identifier>PMID: 23989160</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Amino Acid Sequence ; Binding Sites ; CD40 Ligand - chemistry ; CD40 Ligand - genetics ; CD40 Ligand - isolation & purification ; CD40L ; Cloning ; Combinatorial analysis ; Crystal structure ; Crystallization Communications ; Crystallography, X-Ray ; Diffraction ; Escherichia coli - genetics ; Fibronectin ; fibronectin type III domains ; Fibronectins - chemistry ; Fibronectins - genetics ; Gene Expression ; Human ; Humans ; Molecular Sequence Data ; Peptide Library ; Peptides - chemistry ; Peptides - genetics ; Peptides - isolation & purification ; Protein Binding ; Protein Structure, Secondary ; Proteins ; Purification ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Sequence Alignment</subject><ispartof>Acta crystallographica. 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Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>Tn3 proteins are a novel class of binding molecules based on the third fibronectin type III domain of human tenascin C. Target‐specific Tn3 proteins are selected from combinatorial libraries in which three surface‐exposed loops have been diversified. Here, the cocrystallization of two different Tn3 proteins in complex with CD40L, a therapeutic target for immunological disease, is reported. These crystal structures are the first to be reported of Tn3 proteins and will help to reveal how these engineered molecules achieve specific recognition of a cognate target.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>CD40 Ligand - chemistry</subject><subject>CD40 Ligand - genetics</subject><subject>CD40 Ligand - isolation & purification</subject><subject>CD40L</subject><subject>Cloning</subject><subject>Combinatorial analysis</subject><subject>Crystal structure</subject><subject>Crystallization Communications</subject><subject>Crystallography, X-Ray</subject><subject>Diffraction</subject><subject>Escherichia coli - genetics</subject><subject>Fibronectin</subject><subject>fibronectin type III domains</subject><subject>Fibronectins - chemistry</subject><subject>Fibronectins - genetics</subject><subject>Gene Expression</subject><subject>Human</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Peptide Library</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - isolation & purification</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Purification</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Sequence Alignment</subject><issn>1744-3091</issn><issn>1744-3091</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNqNkk1v1DAQhiMEomXhB3BBlrhwaMCO48TmgFQt7LJixYcAtZwsx5kUl8QOdpZu-D_8T7wfrAocwBd7xs_7ajyeJLlP8GNCcPnkPSnznGJBCMVZxvPyRnK8SaWb3M1r56PkTgiXGFMqCn47Ocqo4IIU-Dj5MTOVdxb0YCwaxh7QYrFAteuUsQGBvTAWwEONBocqY2s0fZ7j5VOkW2eNvThBsO49hGCcPUH9ypvGaDVsI-3HMKi2Nd-3CaSiOrKt6YxVfkTnqVcjqk3TeKX3hGrHYAJyDRquHNKu61tYQ7ib3GpUG-Defp8kH2cvPkxfpss388X0dJlqlvMsZURRRohmuuQNg1wwYEI0uKoYhTrDlQDMCwF5AVjnNBOUFlQVlPFKFYISOkme7Xz7VdVBrcEOXrWy96aLFUunjPz9xprP8sJ9k7RkPPYzGjzaG3j3dQVhkJ0JGtpWWXCrIEme8zLDhIn_QDORES7wxvXhH-ilW_nYrC3Fefz_uCYJ2VHauxA8NIe6CZabeZF_zUvUPLj-4IPi14BEQOyAK9PC-G9Hefpplr2dsxhFbbrTmjDA-qBV_ossytgxefZ6Lufl9Pzs1fSdZPQntgjcFw</recordid><startdate>201309</startdate><enddate>201309</enddate><creator>Oganesyan, Vaheh</creator><creator>Ferguson, Andrew</creator><creator>Grinberg, Luba</creator><creator>Wang, Lin</creator><creator>Phipps, Sandrina</creator><creator>Chacko, Benoy</creator><creator>Drabic, Stacey</creator><creator>Thisted, Thomas</creator><creator>Baca, Manuel</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>7U5</scope><scope>L7M</scope><scope>5PM</scope></search><sort><creationdate>201309</creationdate><title>Fibronectin type III domains engineered to bind CD40L: cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of two complexes</title><author>Oganesyan, Vaheh ; 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Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oganesyan, Vaheh</au><au>Ferguson, Andrew</au><au>Grinberg, Luba</au><au>Wang, Lin</au><au>Phipps, Sandrina</au><au>Chacko, Benoy</au><au>Drabic, Stacey</au><au>Thisted, Thomas</au><au>Baca, Manuel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fibronectin type III domains engineered to bind CD40L: cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of two complexes</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2013-09</date><risdate>2013</risdate><volume>69</volume><issue>9</issue><spage>1045</spage><epage>1048</epage><pages>1045-1048</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><eissn>2053-230X</eissn><abstract>Tn3 proteins are a novel class of binding molecules based on the third fibronectin type III domain of human tenascin C. Target‐specific Tn3 proteins are selected from combinatorial libraries in which three surface‐exposed loops have been diversified. Here, the cocrystallization of two different Tn3 proteins in complex with CD40L, a therapeutic target for immunological disease, is reported. 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| ispartof | Acta crystallographica. Section F, Structural biology and crystallization communications, 2013-09, Vol.69 (9), p.1045-1048 |
| issn | 1744-3091 1744-3091 2053-230X |
| language | eng |
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| subjects | Amino Acid Sequence Binding Sites CD40 Ligand - chemistry CD40 Ligand - genetics CD40 Ligand - isolation & purification CD40L Cloning Combinatorial analysis Crystal structure Crystallization Communications Crystallography, X-Ray Diffraction Escherichia coli - genetics Fibronectin fibronectin type III domains Fibronectins - chemistry Fibronectins - genetics Gene Expression Human Humans Molecular Sequence Data Peptide Library Peptides - chemistry Peptides - genetics Peptides - isolation & purification Protein Binding Protein Structure, Secondary Proteins Purification Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Sequence Alignment |
| title | Fibronectin type III domains engineered to bind CD40L: cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of two complexes |
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