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New page: left|200px<br /> <applet load="1ryu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryu" /> '''Solution Structure of the SWI1 ARID'''<br /...
 
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[[Image:1ryu.gif|left|200px]]<br />
[[Image:1ryu.gif|left|200px]]<br /><applet load="1ryu" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1ryu" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1ryu" />
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'''Solution Structure of the SWI1 ARID'''<br />
'''Solution Structure of the SWI1 ARID'''<br />


==Overview==
==Overview==
ARID (AT-rich interaction domain) is a homologous family of DNA-binding, domains that occur in DNA-binding proteins from a wide variety of species, ranging from yeast to nematodes, insects, mammals, and plants. SWI1, a, member of the SWI/SNF protein complex that is involved in chromatin, remodeling during transcription, contains the ARID motif. The ARID domain, of human SWI1 (also known as p270) does not select for a specific DNA, sequence from a random sequence pool. The lack of sequence specificity, shown by the SWI1 ARID domain stands in contrast to the other, characterized ARID domains, which recognize specific AT-rich sequences. We, have solved the three-dimensional structure of human SWI1 ARID using, solution NMR methods. In addition, we have characterized nonspecific DNA, binding by the SWI1 ARID domain. Results from this study indicate that a, flexible, long, internal loop in the ARID motif is likely to be important, for sequence-specific DNA recognition. The structure of the human SWI1, ARID domain also represents a distinct structural subfamily. Studies of, ARID indicate that the boundary of DNA binding structural and functional, domains can extend beyond the sequence homologous region in a homologous, family of proteins. Structural studies of homologous domains such as the, ARID family of DNA-binding domains should provide information to better, predict the boundary of structural and functional domains in structural, genomic studies.
ARID (AT-rich interaction domain) is a homologous family of DNA-binding domains that occur in DNA-binding proteins from a wide variety of species, ranging from yeast to nematodes, insects, mammals, and plants. SWI1, a member of the SWI/SNF protein complex that is involved in chromatin remodeling during transcription, contains the ARID motif. The ARID domain of human SWI1 (also known as p270) does not select for a specific DNA sequence from a random sequence pool. The lack of sequence specificity shown by the SWI1 ARID domain stands in contrast to the other characterized ARID domains, which recognize specific AT-rich sequences. We have solved the three-dimensional structure of human SWI1 ARID using solution NMR methods. In addition, we have characterized nonspecific DNA binding by the SWI1 ARID domain. Results from this study indicate that a flexible, long, internal loop in the ARID motif is likely to be important for sequence-specific DNA recognition. The structure of the human SWI1 ARID domain also represents a distinct structural subfamily. Studies of ARID indicate that the boundary of DNA binding structural and functional domains can extend beyond the sequence homologous region in a homologous family of proteins. Structural studies of homologous domains such as the ARID family of DNA-binding domains should provide information to better predict the boundary of structural and functional domains in structural genomic studies.


==About this Structure==
==About this Structure==
1RYU 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=1RYU OCA].  
1RYU 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=1RYU OCA].  


==Reference==
==Reference==
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[[Category: swi1]]
[[Category: swi1]]


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Revision as of 15:56, 21 February 2008

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1ryu

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Solution Structure of the SWI1 ARID

OverviewOverview

ARID (AT-rich interaction domain) is a homologous family of DNA-binding domains that occur in DNA-binding proteins from a wide variety of species, ranging from yeast to nematodes, insects, mammals, and plants. SWI1, a member of the SWI/SNF protein complex that is involved in chromatin remodeling during transcription, contains the ARID motif. The ARID domain of human SWI1 (also known as p270) does not select for a specific DNA sequence from a random sequence pool. The lack of sequence specificity shown by the SWI1 ARID domain stands in contrast to the other characterized ARID domains, which recognize specific AT-rich sequences. We have solved the three-dimensional structure of human SWI1 ARID using solution NMR methods. In addition, we have characterized nonspecific DNA binding by the SWI1 ARID domain. Results from this study indicate that a flexible, long, internal loop in the ARID motif is likely to be important for sequence-specific DNA recognition. The structure of the human SWI1 ARID domain also represents a distinct structural subfamily. Studies of ARID indicate that the boundary of DNA binding structural and functional domains can extend beyond the sequence homologous region in a homologous family of proteins. Structural studies of homologous domains such as the ARID family of DNA-binding domains should provide information to better predict the boundary of structural and functional domains in structural genomic studies.

About this StructureAbout this Structure

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

ReferenceReference

Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition., Kim S, Zhang Z, Upchurch S, Isern N, Chen Y, J Biol Chem. 2004 Apr 16;279(16):16670-6. Epub 2004 Jan 13. PMID:14722072

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