2hzd

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|ACTIVITY=
|ACTIVITY=
|GENE= TEAD1, TCF13, TEF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= TEAD1, TCF13, TEF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hzd OCA], [http://www.ebi.ac.uk/pdbsum/2hzd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hzd RCSB]</span>
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==Overview==
==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.
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==Disease==
 
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Known disease associated with this structure: Sveinsson choreoretinal atrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=189967 189967]]
 
==About this Structure==
==About this Structure==
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[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:23:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:37:37 2008''

Revision as of 00:37, 31 March 2008


PDB ID 2hzd

Drag the structure with the mouse to rotate
Gene: TEAD1, TCF13, TEF1 (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR structure of the DNA-binding TEA domain and insights into TEF-1 function


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.

About this Structure

2HZD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain., Anbanandam A, Albarado DC, Nguyen CT, Halder G, Gao X, Veeraraghavan S, Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17225-30. Epub 2006 Nov 3. PMID:17085591

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