1qm9: Difference between revisions

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New page: left|200px<br /> <applet load="1qm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qm9" /> '''NMR, REPRESENTATIVE STRUCTURE'''<br /> ==O...
 
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[[Image:1qm9.gif|left|200px]]<br />
[[Image:1qm9.gif|left|200px]]<br /><applet load="1qm9" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1qm9" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1qm9" />
caption="1qm9" />
'''NMR, REPRESENTATIVE STRUCTURE'''<br />
'''NMR, REPRESENTATIVE STRUCTURE'''<br />


==Overview==
==Overview==
Polypyrimidine tract binding protein (PTB), an RNA binding protein, containing four RNA recognition motifs (RRMs), is involved in both, pre-mRNA splicing and translation initiation directed by picornaviral, internal ribosome entry sites. Sequence comparisons previously indicated, that PTB is a non-canonical RRM protein. The solution structure of a PTB, fragment containing RRMs 3 and 4 shows that the protein consists of two, domains connected by a long, flexible linker. The two domains tumble, independently in solution, having no fixed relative orientation. In, addition to the betaalphabetabetaalphabeta topology, which is, characteristic of RRM domains, the C-terminal extension of PTB RRM-3, incorporates an unanticipated fifth beta-strand, which extends the RNA, binding surface. The long, disordered polypeptide connecting beta4 and, beta5 in RRM-3 is poised above the RNA binding surface and is likely to, contribute to RNA recognition. Mutational analyses show that both RRM-3, and RRM-4 contribute to RNA binding specificity and that, despite its, unusual sequence, PTB binds RNA in a manner akin to that of other RRM, proteins.
Polypyrimidine tract binding protein (PTB), an RNA binding protein containing four RNA recognition motifs (RRMs), is involved in both pre-mRNA splicing and translation initiation directed by picornaviral internal ribosome entry sites. Sequence comparisons previously indicated that PTB is a non-canonical RRM protein. The solution structure of a PTB fragment containing RRMs 3 and 4 shows that the protein consists of two domains connected by a long, flexible linker. The two domains tumble independently in solution, having no fixed relative orientation. In addition to the betaalphabetabetaalphabeta topology, which is characteristic of RRM domains, the C-terminal extension of PTB RRM-3 incorporates an unanticipated fifth beta-strand, which extends the RNA binding surface. The long, disordered polypeptide connecting beta4 and beta5 in RRM-3 is poised above the RNA binding surface and is likely to contribute to RNA recognition. Mutational analyses show that both RRM-3 and RRM-4 contribute to RNA binding specificity and that, despite its unusual sequence, PTB binds RNA in a manner akin to that of other RRM proteins.


==About this Structure==
==About this Structure==
1QM9 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QM9 OCA].  
1QM9 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=1QM9 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Conte, M.R.]]
[[Category: Conte, M R.]]
[[Category: Curry, S.]]
[[Category: Curry, S.]]
[[Category: Grune, T.]]
[[Category: Grune, T.]]
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[[Category: translation]]
[[Category: translation]]


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