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Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double-stranded RNA-binding Protein ZFa

Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double-stranded RNA-binding Protein ZFa

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MÖLLER, Heiko M., Maria A. MARTINEZ-YAMOUT, H. Jane DYSON, Peter E. WRIGHT, 2005. Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double-stranded RNA-binding Protein ZFa. In: Journal of Molecular Biology. 351(4), pp. 718-730. ISSN 0022-2836. eISSN 1089-8638

@article{Moller2005-08-26Solut-21270, title={Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double-stranded RNA-binding Protein ZFa}, year={2005}, doi={10.1016/j.jmb.2005.06.032}, number={4}, volume={351}, issn={0022-2836}, journal={Journal of Molecular Biology}, pages={718--730}, author={Möller, Heiko M. and Martinez-Yamout, Maria A. and Dyson, H. Jane and Wright, Peter E.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/21270"> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/21270"/> <dc:contributor>Martinez-Yamout, Maria A.</dc:contributor> <dc:contributor>Wright, Peter E.</dc:contributor> <dc:creator>Dyson, H. Jane</dc:creator> <dc:language>eng</dc:language> <dc:contributor>Dyson, H. Jane</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-01-28T09:22:49Z</dc:date> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:creator>Wright, Peter E.</dc:creator> <dc:contributor>Möller, Heiko M.</dc:contributor> <dcterms:bibliographicCitation>Journal of Molecular Biology ; 351 (2005), 4. - S. 718-730</dcterms:bibliographicCitation> <dcterms:abstract>Several zinc finger proteins have been discovered recently that bind specifically to double-stranded RNA. These include the mammalian JAZ and wig proteins, and the seven-zinc finger protein ZFa from Xenopus laevis. We have determined the solution structure of a 127 residue fragment of ZFa, which consists of two zinc finger domains connected by a linker that remains unstructured in the free protein in solution. The first zinc finger consists of a three-stranded beta-sheet and three helices, while the second finger contains only a two-stranded sheet and two helices. The common structures of the core regions of the two fingers are superimposable. Each finger has a highly electropositive surface that maps to a helix-kink-helix motif. There is no evidence for interactions between the two fingers, consistent with the length (24 residues) and unstructured nature of the intervening linker. Comparison with a number of other proteins shows similarities in the topology and arrangement of secondary structure elements with canonical DNA-binding zinc fingers, with protein interaction motifs such as FOG zinc fingers, and with other DNA-binding and RNA-binding proteins that do not contain zinc. However, in none of these cases does the alignment of these structures with the ZFa zinc fingers produce a consistent picture of a plausible RNA-binding interface. We conclude that the ZFa zinc fingers represent a new motif for the binding of double-stranded RNA.</dcterms:abstract> <dcterms:issued>2005-08-26</dcterms:issued> <dc:creator>Martinez-Yamout, Maria A.</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-01-28T09:22:49Z</dcterms:available> <dcterms:title>Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double-stranded RNA-binding Protein ZFa</dcterms:title> <dc:creator>Möller, Heiko M.</dc:creator> </rdf:Description> </rdf:RDF>

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