1ryu: Difference between revisions
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 /... |
No edit summary |
||
Line 1: | Line 1: | ||
[[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=" | |||
caption="1ryu" /> | caption="1ryu" /> | ||
'''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 | 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:// | 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== | ||
Line 25: | Line 24: | ||
[[Category: swi1]] | [[Category: swi1]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:00 2008'' |
Revision as of 15:56, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 14:56:00 2008