1mp1

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(New page: 200px<br /> <applet load="1mp1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mp1" /> '''Solution structure of the PWI motif from SR...)
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'''Solution structure of the PWI motif from SRm160'''<br />
'''Solution structure of the PWI motif from SRm160'''<br />
==Overview==
==Overview==
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The PWI motif is a highly conserved domain of unknown function in the, SRm160 splicing and 3'-end cleavage-stimulatory factor, as well as in, several other known or putative pre-mRNA processing components. We show, here that the PWI motif is a new type of RNA/DNA-binding domain that has, an equal preference for single- and double-stranded nucleic acids., Deletion of the motif prevents SRm160 from binding RNA and stimulating, 3'-end cleavage, and its substitution with a heterologous RNA-binding, domain restores these functions. The NMR solution structure of the, SRm160-PWI motif reveals a novel, four-helix bundle and represents the, first example of an alpha-helical fold that can bind single-stranded, (ss)RNA. Structure-guided mutagenesis indicates that the same surface is, involved in RNA and DNA binding and requires the cooperative action of a, highly conserved, adjacent basic region. Thus, the PWI motif is a novel, type of nucleic acid-binding domain that likely has multiple important, functions in pre-mRNA processing, including SRm160-dependent stimulation, of 3'-end formation.
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The PWI motif is a highly conserved domain of unknown function in the SRm160 splicing and 3'-end cleavage-stimulatory factor, as well as in several other known or putative pre-mRNA processing components. We show here that the PWI motif is a new type of RNA/DNA-binding domain that has an equal preference for single- and double-stranded nucleic acids. Deletion of the motif prevents SRm160 from binding RNA and stimulating 3'-end cleavage, and its substitution with a heterologous RNA-binding domain restores these functions. The NMR solution structure of the SRm160-PWI motif reveals a novel, four-helix bundle and represents the first example of an alpha-helical fold that can bind single-stranded (ss)RNA. Structure-guided mutagenesis indicates that the same surface is involved in RNA and DNA binding and requires the cooperative action of a highly conserved, adjacent basic region. Thus, the PWI motif is a novel type of nucleic acid-binding domain that likely has multiple important functions in pre-mRNA processing, including SRm160-dependent stimulation of 3'-end formation.
==About this Structure==
==About this Structure==
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1MP1 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=1MP1 OCA].
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1MP1 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=1MP1 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arrowsmith, C.H.]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Blencowe, B.J.]]
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[[Category: Blencowe, B J.]]
[[Category: Bowman, J.]]
[[Category: Bowman, J.]]
[[Category: Cox, B.]]
[[Category: Cox, B.]]
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[[Category: Graveley, B.R.]]
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[[Category: Graveley, B R.]]
[[Category: Lambermon, M.]]
[[Category: Lambermon, M.]]
[[Category: Lu, Y.]]
[[Category: Lu, Y.]]
[[Category: McCracken, S.]]
[[Category: McCracken, S.]]
[[Category: Pineda-Lucena, A.]]
[[Category: Pineda-Lucena, A.]]
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[[Category: Szymczyna, B.R.]]
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[[Category: Szymczyna, B R.]]
[[Category: four helix bundle]]
[[Category: four helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:31 2008''

Revision as of 11:57, 21 February 2008


1mp1

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Solution structure of the PWI motif from SRm160

Overview

The PWI motif is a highly conserved domain of unknown function in the SRm160 splicing and 3'-end cleavage-stimulatory factor, as well as in several other known or putative pre-mRNA processing components. We show here that the PWI motif is a new type of RNA/DNA-binding domain that has an equal preference for single- and double-stranded nucleic acids. Deletion of the motif prevents SRm160 from binding RNA and stimulating 3'-end cleavage, and its substitution with a heterologous RNA-binding domain restores these functions. The NMR solution structure of the SRm160-PWI motif reveals a novel, four-helix bundle and represents the first example of an alpha-helical fold that can bind single-stranded (ss)RNA. Structure-guided mutagenesis indicates that the same surface is involved in RNA and DNA binding and requires the cooperative action of a highly conserved, adjacent basic region. Thus, the PWI motif is a novel type of nucleic acid-binding domain that likely has multiple important functions in pre-mRNA processing, including SRm160-dependent stimulation of 3'-end formation.

About this Structure

1MP1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing., Szymczyna BR, Bowman J, McCracken S, Pineda-Lucena A, Lu Y, Cox B, Lambermon M, Graveley BR, Arrowsmith CH, Blencowe BJ, Genes Dev. 2003 Feb 15;17(4):461-75. PMID:12600940

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