Literature DB >> 2479579

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

A Ghetti1, C Padovani, G Di Cesare, C Morandi.   

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.

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Year:  1989        PMID: 2479579     DOI: 10.1016/0014-5793(89)81575-3

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  5 in total

1.  RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.

Authors:  D W Hoffman; C C Query; B L Golden; S W White; J D Keene
Journal:  Proc Natl Acad Sci U S A       Date:  1991-03-15       Impact factor: 11.205

2.  Modelling by homology of RNA binding domain.

Authors:  A Ghetti; M Bolognesi; F Cobianchi; C Morandi
Journal:  Mol Biol Rep       Date:  1990       Impact factor: 2.316

3.  Defining the orientation of the human U1A RBD1 on its UTR by tethered-EDTA(Fe) cleavage.

Authors:  D L Beck; W T Stump; K B Hall
Journal:  RNA       Date:  1998-03       Impact factor: 4.942

4.  The U2B'' RNP motif as a site of protein-protein interaction.

Authors:  D Scherly; N A Dathan; W Boelens; W J van Venrooij; I W Mattaj
Journal:  EMBO J       Date:  1990-11       Impact factor: 11.598

5.  Interaction of N-terminal domain of U1A protein with an RNA stem/loop.

Authors:  K B Hall; W T Stump
Journal:  Nucleic Acids Res       Date:  1992-08-25       Impact factor: 16.971

  5 in total

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