1p1t
From Proteopedia
(New page: 200px<br /> <applet load="1p1t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p1t" /> '''NMR Structure of the N-terminal RRM domain ...) |
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'''NMR Structure of the N-terminal RRM domain of Cleavage stimulation factor 64 KDa subunit'''<br /> | '''NMR Structure of the N-terminal RRM domain of Cleavage stimulation factor 64 KDa subunit'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P1T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1P1T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P1T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rna recognition motif]] | [[Category: rna recognition motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:38:15 2008'' |
Revision as of 14:38, 15 February 2008
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NMR Structure of the N-terminal RRM domain of Cleavage stimulation factor 64 KDa subunit
Overview
Vertebrate polyadenylation sites are identified by the AAUAAA signal and, by GU-rich sequences downstream of the cleavage site. These are recognized, by a heterotrimeric protein complex (CstF) through its 64 kDa subunit, (CstF-64); the strength of this interaction affects the efficiency of, poly(A) site utilization. We present the structure of the RNA-binding, domain of CstF-64 containing an RNA recognition motif (RRM) augmented by, N- and C-terminal helices. The C-terminal helix unfolds upon RNA binding, and extends into the hinge domain where interactions with factors, responsible for assembly of the polyadenylation complex occur. We propose, that this conformational change initiates assembly. Consecutive Us are, required for a strong CstF-GU interaction and we show how UU dinucleotides, are recognized. Contacts outside the UU pocket fine tune the protein-RNA, interaction and provide different affinities for distinct GU-rich, elements. The protein-RNA interface remains mobile, most likely a, requirement to bind many GU-rich sequences and yet discriminate against, other RNAs. The structural distinction between sequences that form stable, and unstable complexes provides an operational distinction between weakly, and strongly processed poly(A) sites.
About this Structure
1P1T is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein., Perez Canadillas JM, Varani G, EMBO J. 2003 Jun 2;22(11):2821-30. PMID:12773396
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