1qm9
From Proteopedia
(New page: 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=" | + | |
caption="1qm9" /> | caption="1qm9" /> | ||
'''NMR, REPRESENTATIVE STRUCTURE'''<br /> | '''NMR, REPRESENTATIVE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Polypyrimidine tract binding protein (PTB), an RNA binding protein | + | 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:// | + | 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 | + | [[Category: Conte, M R.]] |
[[Category: Curry, S.]] | [[Category: Curry, S.]] | ||
[[Category: Grune, T.]] | [[Category: Grune, T.]] | ||
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[[Category: translation]] | [[Category: translation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:15 2008'' |
Revision as of 12:41, 21 February 2008
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NMR, REPRESENTATIVE STRUCTURE
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.
About this Structure
1QM9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold., Conte MR, Grune T, Ghuman J, Kelly G, Ladas A, Matthews S, Curry S, EMBO J. 2000 Jun 15;19(12):3132-41. PMID:10856256
Page seeded by OCA on Thu Feb 21 14:41:15 2008
