2err

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(New page: 200px<br /> <applet load="2err" size="450" color="white" frame="true" align="right" spinBox="true" caption="2err" /> '''NMR Structure of the RNA Binding Domain of ...)
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'''NMR Structure of the RNA Binding Domain of Human Fox-1 in Complex with UGCAUGU'''<br />
'''NMR Structure of the RNA Binding Domain of Human Fox-1 in Complex with UGCAUGU'''<br />
==Overview==
==Overview==
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The Fox-1 protein regulates alternative splicing of tissue-specific exons, by binding to GCAUG elements. Here, we report the solution structure of, the Fox-1 RNA binding domain (RBD) in complex with UGCAUGU. The last three, nucleotides, UGU, are recognized in a canonical way by the four-stranded, beta-sheet of the RBD. In contrast, the first four nucleotides, UGCA, are, bound by two loops of the protein in an unprecedented manner. Nucleotides, U1, G2, and C3 are wrapped around a single phenylalanine, while G2 and A4, form a base-pair. This novel RNA binding site is independent from the, beta-sheet binding interface. Surface plasmon resonance analyses were used, to quantify the energetic contributions of electrostatic and hydrogen bond, interactions to complex formation and support our structural findings., These results demonstrate the unusual molecular mechanism of, sequence-specific RNA recognition by Fox-1, which is exceptional in its, high affinity for a defined but short sequence element.
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The Fox-1 protein regulates alternative splicing of tissue-specific exons by binding to GCAUG elements. Here, we report the solution structure of the Fox-1 RNA binding domain (RBD) in complex with UGCAUGU. The last three nucleotides, UGU, are recognized in a canonical way by the four-stranded beta-sheet of the RBD. In contrast, the first four nucleotides, UGCA, are bound by two loops of the protein in an unprecedented manner. Nucleotides U1, G2, and C3 are wrapped around a single phenylalanine, while G2 and A4 form a base-pair. This novel RNA binding site is independent from the beta-sheet binding interface. Surface plasmon resonance analyses were used to quantify the energetic contributions of electrostatic and hydrogen bond interactions to complex formation and support our structural findings. These results demonstrate the unusual molecular mechanism of sequence-specific RNA recognition by Fox-1, which is exceptional in its high affinity for a defined but short sequence element.
==About this Structure==
==About this Structure==
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2ERR 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=2ERR OCA].
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2ERR 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=2ERR OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Allain, F.H.]]
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[[Category: Allain, F H.]]
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[[Category: Auweter, S.D.]]
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[[Category: Auweter, S D.]]
[[Category: protein-rna complex]]
[[Category: protein-rna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:55 2008''

Revision as of 15:13, 21 February 2008


2err

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NMR Structure of the RNA Binding Domain of Human Fox-1 in Complex with UGCAUGU

Overview

The Fox-1 protein regulates alternative splicing of tissue-specific exons by binding to GCAUG elements. Here, we report the solution structure of the Fox-1 RNA binding domain (RBD) in complex with UGCAUGU. The last three nucleotides, UGU, are recognized in a canonical way by the four-stranded beta-sheet of the RBD. In contrast, the first four nucleotides, UGCA, are bound by two loops of the protein in an unprecedented manner. Nucleotides U1, G2, and C3 are wrapped around a single phenylalanine, while G2 and A4 form a base-pair. This novel RNA binding site is independent from the beta-sheet binding interface. Surface plasmon resonance analyses were used to quantify the energetic contributions of electrostatic and hydrogen bond interactions to complex formation and support our structural findings. These results demonstrate the unusual molecular mechanism of sequence-specific RNA recognition by Fox-1, which is exceptional in its high affinity for a defined but short sequence element.

About this Structure

2ERR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular basis of RNA recognition by the human alternative splicing factor Fox-1., Auweter SD, Fasan R, Reymond L, Underwood JG, Black DL, Pitsch S, Allain FH, EMBO J. 2006 Jan 11;25(1):163-73. Epub 2005 Dec 15. PMID:16362037

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