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PMID: 9646873 Published · ppublish English Journal Article Review

RNA recognition by RNP proteins during RNA processing.

Annual review of biophysics and biomolecular structure ·Vol. 27 ·1998-00-00 ·Pages 407-45

Varani G, Nagai K

Abstract

The ribonucleoprotein (RNP) domain is one of the most common eukaryotic protein folds. Proteins containing RNP domains function in important steps of posttranscriptional regulation of gene expression by directing the assembly of multiprotein complexes on primary transcripts, mature mRNAs, and stable ribonucleoprotein components of the RNA processing machinery. The diverse functions performed by these proteins depend on their dual ability to recognize RNA and to interact with other proteins, often utilizing specialized auxiliary domains. Crystallographic and NMR structures of several RNP domains and a handful of structures of RNA-protein complexes have begun to reveal the molecular basis for RNP-RNA recognition.

MeSH Terms
Alternative Splicing Amino Acid Sequence Animals Base Sequence Binding Sites Gene Expression Regulation Humans Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Biosynthesis Protein Conformation Proteins/chemistry RNA/biosynthesis,chemistry,genetics RNA Processing, Post-Transcriptional RNA, Messenger/chemistry,metabolism Ribonucleoproteins/chemistry,metabolism Transcription, Genetic
Chemicals
Proteins RNA, Messenger Ribonucleoproteins RNA
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Varani G
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom. [email protected]
Nagai K
Article Info
Journal
Annual review of biophysics and biomolecular structure
Abbr.
Annu Rev Biophys Biomol Struct
ISSN
1056-8700
Published
1998-00-00
Pages
407-45
Language
English
Region
United States
NLM ID
9211097
Subset
IM
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