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Secondary structure prediction for RNA binding domain in RNP proteins identifies βαβ as the main structural motif
Author(s) -
Ghetti A.,
Padovani C.,
Di Cesare G.,
Morandi C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81575-3
Subject(s) - rna , rna binding protein , protein secondary structure , computational biology , signal recognition particle rna , binding domain , nucleic acid secondary structure , ribonucleoprotein , rna recognition motif , biology , microbiology and biotechnology , chemistry , binding site , genetics , biochemistry , gene
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.