Structure-function relationships of the polypyrimidine tract binding protein |
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Authors: | Auweter S D Allain F H-T |
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Institution: | (1) Institute for Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland;(2) Present address: Michael Smith Laboratories, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada |
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Abstract: | The polypyrimidine tract binding protein (PTB) is a 58-kDa RNA binding protein involved in multiple aspects of mRNA metabolism
including splicing regulation, polyadenylation, 3′end formation, internal ribosomal entry site-mediated translation, RNA localization
and stability. PTB contains four RNA recognition motifs (RRMs) separated by three linkers. In this review we summarize structural
information on PTB in solution that has been gathered during the past 7 years using NMR spectroscopy and small-angle X-ray
scattering. The structures of all RRMs of PTB in their free state and in complex with short pyrimidine tracts, as well as
a structural model of PTB RRM2 in complex with a peptide, revealed unusual structural features that provided new insights
into the mechanisms of action of PTB in the different processes of RNA metabolism and in particular splicing regulation.
Received 16 August 2007; received after revision 18 September 2007; accepted 2 October 2007 |
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Keywords: | Alternative splicing translation regulation polypyrimidine tract binding protein RNA-protein complex RNA-protein recognition RNA recognition motifs RBD splicing regulation |
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