Crystal structures of a series of RNA aptamers complexed to the same protein target
We have determined the crystal structures, at 2.8 Å resolution, of two different RNA aptamers, each bound to MS2 coat protein. One of the aptamers contains a non-Watson-Crick base pair, while the other is missing one of the unpaired adenines that make sequence-specific contacts in the wild-type comp...
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| Veröffentlicht in: | Nature Structural Biology 1998-11, Vol.5 (11), p.970-975 |
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| container_end_page | 975 |
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| container_issue | 11 |
| container_start_page | 970 |
| container_title | Nature Structural Biology |
| container_volume | 5 |
| creator | Phillips, Simon E.V Rowsell, Siân Stonehouse, Nicola J Convery, Máire A Adams, Chris J Ellington, Andrew D Hirao, Ichiro Peabody, David S Stockley, Peter G |
| description | We have determined the crystal structures, at 2.8 Å resolution, of two different RNA aptamers, each bound to MS2 coat protein. One of the aptamers contains a non-Watson-Crick base pair, while the other is missing one of the unpaired adenines that make sequence-specific contacts in the wild-type complex. Despite these differences, the RNA aptamers bind in the same location on the protein as the wild-type translational operator. Comparison of these new structures with other MS2-RNA complexes allows us to refine further the definition of the minimal recognition elements and suggests a possible application of the MS2 system for routine structure determination of small nucleic acid motifs. |
| doi_str_mv | 10.1038/2946 |
| format | Article |
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Comparison of these new structures with other MS2-RNA complexes allows us to refine further the definition of the minimal recognition elements and suggests a possible application of the MS2 system for routine structure determination of small nucleic acid motifs.</description><subject>Base Pairing</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Capsid - chemistry</subject><subject>Capsid Proteins</subject><subject>Crystallography, X-Ray</subject><subject>Hydrogen Bonding</subject><subject>letter</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Nucleic Acid Conformation</subject><subject>Phage MS2</subject><subject>Protein Structure</subject><subject>RNA - chemistry</subject><subject>RNA-Binding Proteins - chemistry</subject><issn>1072-8368</issn><issn>2331-365X</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFtLwzAYhoMoc27-BCGCelfNqU16KcMTDAUP4F1J06-zo4eZpOD-vSkdu_BGAknI-_B-5EFoTsk1JVzdsFQkB2jKOKcRT-LPQzSlRLJI8UQdoxPn1oRQIUg6QZNUEUUEm6K3hd06r2vsvO2N7y043JVYYwe2Gu-vz7dYb7xuwDpsumZTww8U2HfYfwF24R1vbOeharHXdgV-jo5KXTs43Z0z9HF_9754jJYvD0-L22VkeCx92I3ikOYFVbkUPGHDYkrHpS4lT0Akihmj4yI2StISRMpk-AtXJag4yTmfoauxN4z_7sH5rKmcgbrWLXS9yyQhnAkS_wtSyZI4VTKAFyNobOechTLb2KrRdptRkg2Ss0FywM52fX3eQLGHdlZDfjnmLiTtCmy27nrbBhd_e85HrtWD-X1P63JKU5WlkvBfmtaMvw</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Phillips, Simon E.V</creator><creator>Rowsell, Siân</creator><creator>Stonehouse, Nicola J</creator><creator>Convery, Máire A</creator><creator>Adams, Chris J</creator><creator>Ellington, Andrew D</creator><creator>Hirao, Ichiro</creator><creator>Peabody, David S</creator><creator>Stockley, Peter G</creator><general>Nature Publishing Group US</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19981101</creationdate><title>Crystal structures of a series of RNA aptamers complexed to the same protein target</title><author>Phillips, Simon E.V ; 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One of the aptamers contains a non-Watson-Crick base pair, while the other is missing one of the unpaired adenines that make sequence-specific contacts in the wild-type complex. Despite these differences, the RNA aptamers bind in the same location on the protein as the wild-type translational operator. Comparison of these new structures with other MS2-RNA complexes allows us to refine further the definition of the minimal recognition elements and suggests a possible application of the MS2 system for routine structure determination of small nucleic acid motifs.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>9808042</pmid><doi>10.1038/2946</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 1072-8368 |
| ispartof | Nature Structural Biology, 1998-11, Vol.5 (11), p.970-975 |
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| language | eng |
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| subjects | Base Pairing Biochemistry Biological Microscopy Biomedical and Life Sciences Capsid - chemistry Capsid Proteins Crystallography, X-Ray Hydrogen Bonding letter Life Sciences Membrane Biology Models, Molecular Nucleic Acid Conformation Phage MS2 Protein Structure RNA - chemistry RNA-Binding Proteins - chemistry |
| title | Crystal structures of a series of RNA aptamers complexed to the same protein target |
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