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New page: left|200px<br /> <applet load="2com" size="450" color="white" frame="true" align="right" spinBox="true" caption="2com" /> '''The solution structure of the SWIRM domain ...
 
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[[Image:2com.gif|left|200px]]<br />
[[Image:2com.gif|left|200px]]<br /><applet load="2com" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2com" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2com" />
caption="2com" />
'''The solution structure of the SWIRM domain of human LSD1'''<br />
'''The solution structure of the SWIRM domain of human LSD1'''<br />


==Overview==
==Overview==
SWIRM is an evolutionarily conserved domain involved in several, chromatin-modifying complexes. Recently, the LSD1 protein, which bears a, SWIRM domain, was found to be a demethylase for Lys4-methylated histone, H3. Here, we report a solution structure of the SWIRM domain of human, LSD1. It forms a compact fold composed of 6 alpha helices, in which a 20, amino acid long helix (alpha4) is surrounded by 5 other short helices. The, SWIRM domain structure could be divided into the N-terminal part, (alpha1-alpha3) and the C-terminal part (alpha4-alpha6), which are, connected to each other by a salt bridge. While the N-terminal part forms, a SWIRM-specific structure, the C-terminal part adopts a helix-turn-helix, (HTH)-related fold. We discuss a model in which the SWIRM domain acts as, an anchor site for a histone tail.
SWIRM is an evolutionarily conserved domain involved in several chromatin-modifying complexes. Recently, the LSD1 protein, which bears a SWIRM domain, was found to be a demethylase for Lys4-methylated histone H3. Here, we report a solution structure of the SWIRM domain of human LSD1. It forms a compact fold composed of 6 alpha helices, in which a 20 amino acid long helix (alpha4) is surrounded by 5 other short helices. The SWIRM domain structure could be divided into the N-terminal part (alpha1-alpha3) and the C-terminal part (alpha4-alpha6), which are connected to each other by a salt bridge. While the N-terminal part forms a SWIRM-specific structure, the C-terminal part adopts a helix-turn-helix (HTH)-related fold. We discuss a model in which the SWIRM domain acts as an anchor site for a histone tail.


==About this Structure==
==About this Structure==
2COM 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=2COM OCA].  
2COM 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=2COM OCA].  


==Reference==
==Reference==
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[[Category: Kigawa, T.]]
[[Category: Kigawa, T.]]
[[Category: Koshiba, S.]]
[[Category: Koshiba, S.]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Tanaka, A.]]
[[Category: Tanaka, A.]]
[[Category: Tochio, N.]]
[[Category: Tochio, N.]]
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[[Category: swirm domain]]
[[Category: swirm domain]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:50:54 2008''