RNA recognition: towards identifying determinants of specificity

Daniel J. Kenan; Charles C. Query; Jack D. Keene

doi:10.1016/0968-0004(91)90088-D

RNA recognition: towards identifying determinants of specificity

Daniel J. Kenan, Charles C. Query, Jack D. Keene

Research output: Contribution to journal › Article › peer-review

688 Scopus citations

Abstract

Members of a family of proteins containing a conserved ∼80-amino acid RNA recognition motif (RRM) bind specifically to a wide variety of RNA molecules. Structural studies, in combination with sequence alignments, indicate the structural context of both conserved and non-conserved elements in the motif. These analyses suggest that all RRM proteins share a common fold and a similar protein-RNA interface, and that non-conserved residues contribute additional contacts for sequence-specific RNA recognition.

Original language	English (US)
Pages (from-to)	214-220
Number of pages	7
Journal	Trends in Biochemical Sciences
Volume	16
Issue number	C
DOIs	https://doi.org/10.1016/0968-0004(91)90088-D
State	Published - 1991
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.1016/0968-0004(91)90088-D

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abstract = "Members of a family of proteins containing a conserved ∼80-amino acid RNA recognition motif (RRM) bind specifically to a wide variety of RNA molecules. Structural studies, in combination with sequence alignments, indicate the structural context of both conserved and non-conserved elements in the motif. These analyses suggest that all RRM proteins share a common fold and a similar protein-RNA interface, and that non-conserved residues contribute additional contacts for sequence-specific RNA recognition.",

author = "Kenan, {Daniel J.} and Query, {Charles C.} and Keene, {Jack D.}",

year = "1991",

doi = "10.1016/0968-0004(91)90088-D",

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AU - Query, Charles C.

AU - Keene, Jack D.

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AB - Members of a family of proteins containing a conserved ∼80-amino acid RNA recognition motif (RRM) bind specifically to a wide variety of RNA molecules. Structural studies, in combination with sequence alignments, indicate the structural context of both conserved and non-conserved elements in the motif. These analyses suggest that all RRM proteins share a common fold and a similar protein-RNA interface, and that non-conserved residues contribute additional contacts for sequence-specific RNA recognition.

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RNA recognition: towards identifying determinants of specificity

Abstract

ASJC Scopus subject areas

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