1bhi

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[[Image:1bhi.gif|left|200px]]<br /><applet load="1bhi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bhi.gif|left|200px]]
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caption="1bhi" />
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'''STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES'''<br />
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{{Structure
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|PDB= 1bhi |SIZE=350|CAPTION= <scene name='initialview01'>1bhi</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BHI 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=1BHI OCA].
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1BHI is a [[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=1BHI OCA].
==Reference==
==Reference==
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Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain., Nagadoi A, Nakazawa K, Uda H, Okuno K, Maekawa T, Ishii S, Nishimura Y, J Mol Biol. 1999 Apr 2;287(3):593-607. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10092462 10092462]
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Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain., Nagadoi A, Nakazawa K, Uda H, Okuno K, Maekawa T, Ishii S, Nishimura Y, J Mol Biol. 1999 Apr 2;287(3):593-607. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10092462 10092462]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zn finger]]
[[Category: zn finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:11:04 2008''

Revision as of 08:11, 20 March 2008


PDB ID 1bhi

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Gene: CDNA (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES


Overview

Activating transcription factor-2 (ATF-2) is a transcription factor that binds to cAMP response element (CRE). ATF-2 contains two functional domains, an N-terminal transactivation domain and a C-terminal DNA-binding domain. The DNA-binding domain contains the basic leucine zipper (bZip) motif. Here, the three-dimensional structure of the transactivation domain of ATF-2 has been determined by NMR. The transactivation domain consists of two subdomains: the structure of an N-terminal half (N-subdomain) is well determined, while a C-terminal half (C-subdomain) takes a highly flexible and disordered structure. The architecture of the N-subdomain is very similar to that of the well-known zinc finger motif found in DNA-binding domains, consisting of an antiparallel beta-sheet and an alpha-helix. The zinc atom is tetrahedrally coordinated to two cysteine residues and two histidine residues. Amino acids that form the hydrophobic core in all of the DNA-binding zinc fingers are well conserved in the N-subdomain of the transactivation domain, whereas some amino acids that are responsible for binding to the phosphate backbone of DNA in the DNA-binding zinc fingers are substituted with other amino acids. The flexible C-subdomain, which contains two threonine residues that the stress-activated protein kinases phosphorylate, is likely to undergo a conformational change by specific binding to a target protein.

About this Structure

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

Reference

Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain., Nagadoi A, Nakazawa K, Uda H, Okuno K, Maekawa T, Ishii S, Nishimura Y, J Mol Biol. 1999 Apr 2;287(3):593-607. PMID:10092462

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