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PMID: 2479579 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Secondary structure prediction for RNA binding domain in RNP proteins identifies beta alpha beta as the main structural motif.

FEBS letters ·Vol. 257 ·No. 2 ·1989-11-06 ·Pages 373-6

Ghetti A, Padovani C, Di Cesare G, Morandi C

Abstract

In eukaryotic cells transcript processing is strictly dependent upon binding of specific proteins. Nuclear RNA binding proteins share a common domain, which is involved in RNA binding. In order to characterize RNP-RNA interactions we have performed a secondary structure prediction based both on statistical algorithms and comparative analysis of different proteins. A high conservation for secondary structure propensity between different RNPs was observed.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Computer Simulation Humans Hydrogen Bonding Molecular Sequence Data Protein Conformation RNA/metabolism Ribonucleoproteins/ultrastructure
Chemicals
Ribonucleoproteins RNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ghetti A
Istituto di Scienze Biologiche, Università di Verona, Italy.
Padovani C
Di Cesare G
Morandi C
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1989-11-06
Pages
373-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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