Recognition of polyadenylate RNA by the poly(A)-binding protein
Article Abstract:
Polyadenylate RNA and its recognition by the poly(A)-binding protein are discussed. The X-ray structure of an active, C-terminal truncation of human PABP bound to polyadenylate RNA at 2.6-angstrom resolution is presented. Minimal PABP consisting of the N-terminal two RRM-type RNA-binding domains connected by a short linker, RRM1/2 was used for study. The 3-D structure of the unusual protein-nucleic acid complex sheds light on how two RRMs can make a continuous RNA-recognition surface that mediates specific, high-affinity binding to polyadenylate RNA.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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U2AF homology motifs: protein recognition in the RRM world
Article Abstract:
The critical sequence features necessary to mediate protein-U2AF homology motifs (UHMs) interactions, and perform comprehensive database searches to identify new members of the UHM family are reviewed. The resulting implications for the functional and evolutionary relationships among candidate UHM family members are discussed revealing that UHMs represent a novel family of modular protein interaction domains.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2004
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