2hzd: Difference between revisions

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[[Image:2hzd.gif|left|200px]]<br />

[[Image:2hzd.gif|left|200px]]<br /><applet load="2hzd" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2hzd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2hzd" />

'''NMR structure of the DNA-binding TEA domain and insights into TEF-1 function'''<br />

==Overview==

Transcription enhancer factor 1 is essential for cardiac, skeletal, and, smooth muscle development and uses its N-terminal TEA domain (TEAD) to, bind M-CAT elements. Here, we present the first structure of TEAD and show, that it is a three-helix bundle with a homeodomain fold. Structural data, reveal how TEAD binds DNA. Using structure-function correlations, we find, that the L1 loop is essential for cooperative loading of TEAD molecules on, to tandemly duplicated M-CAT sites. Furthermore, using a microarray, chip-based assay, we establish that known binding sites of the full-length, protein are only a subset of DNA elements recognized by TEAD. Our results, provide a model for understanding the regulation of genome-wide gene, expression during development by TEA/ATTS family of transcription factors.

Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA/ATTS family of transcription factors.

==Disease==

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==About this Structure==

2HZD 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=2HZD OCA].

2HZD 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=2HZD OCA].

==Reference==

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[[Category: helix-turn-helix]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:38:~~57 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2hzd.gif|left|200px]]<br />
+[[Image:2hzd.gif|left|200px]]<br /><applet load="2hzd" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2hzd" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2hzd" />
 '''NMR structure of the DNA-binding TEA domain and insights into TEF-1 function'''<br />
 ==Overview==
-Transcription enhancer factor 1 is essential for cardiac, skeletal, and, smooth muscle development and uses its N-terminal TEA domain (TEAD) to, bind M-CAT elements. Here, we present the first structure of TEAD and show, that it is a three-helix bundle with a homeodomain fold. Structural data, reveal how TEAD binds DNA. Using structure-function correlations, we find, that the L1 loop is essential for cooperative loading of TEAD molecules on, to tandemly duplicated M-CAT sites. Furthermore, using a microarray, chip-based assay, we establish that known binding sites of the full-length, protein are only a subset of DNA elements recognized by TEAD. Our results, provide a model for understanding the regulation of genome-wide gene, expression during development by TEA/ATTS family of transcription factors.
+Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA/ATTS family of transcription factors.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-HZD 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=2HZD OCA].
+HZD 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=2HZD OCA].
 ==Reference==
@@ Line 22: / Line 21: @@
 [[Category: helix-turn-helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:38:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:28 2008''