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1nwq

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[[Image:1nwq.gif|left|200px]]
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[[Image:1nwq.png|left|200px]]
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{{STRUCTURE_1nwq| PDB=1nwq | SCENE= }}
{{STRUCTURE_1nwq| PDB=1nwq | SCENE= }}
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'''CRYSTAL STRUCTURE OF C/EBPALPHA-DNA COMPLEX'''
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===CRYSTAL STRUCTURE OF C/EBPALPHA-DNA COMPLEX===
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==Overview==
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CCAAT/enhancer-binding proteins (C/EBPs) are basic region leucine zipper (bZIP) transcription factors that regulate cell differentiation, growth, survival, and inflammation. To understand the molecular basis of DNA recognition by the C/EBP family we determined the x-ray structure of a C/EBPalpha bZIP polypeptide bound to its cognate DNA site (A(-5)T(-4)T(-3)G(-2)C(-1)G(1)C(2)A(3)A(4)T(5)) and characterized several basic region mutants. Binding specificity is provided by interactions of basic region residues Arg(289), Asn(292), Ala(295), Val(296), Ser(299), and Arg(300) with DNA bases. A striking feature of the C/EBPalpha protein-DNA interface that distinguishes it from known bZIP-DNA complexes is the central role of Arg(289), which is hydrogen-bonded to base A(3), phosphate, Asn(292) (invariant in bZIPs), and Asn(293). The conformation of Arg(289) is also restricted by Tyr(285). In accordance with the structural model, mutation of Arg(289) or a pair of its interacting partners (Tyr(285) and Asn(293)) abolished C/EBPalpha binding activity. Val(296) (Ala in most other bZIPs) contributes to C/EBPalpha specificity by discriminating against purines at position -3 and imposing steric restraints on the invariant Arg(300). Mutating Val(296) to Ala strongly enhanced C/EBPalpha binding to cAMP response element (CRE) sites while retaining affinity for C/EBP sites. Thus, Arg(289) is essential for formation of the complementary protein-DNA interface, whereas Val(296) functions primarily to restrict interactions with related sequences such as CRE sites rather than specifying binding to C/EBP sites. Our studies also help to explain the phenotypes of mice carrying targeted mutations in the C/EBPalpha bZIP region.
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(as it appears on PubMed at http://www.pubmed.gov), where 12578822 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12578822}}
==About this Structure==
==About this Structure==
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[[Category: Basic leucine zipper]]
[[Category: Basic leucine zipper]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:04:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:26:36 2008''

Revision as of 12:26, 27 July 2008

Image:1nwq.png

Template:STRUCTURE 1nwq

CRYSTAL STRUCTURE OF C/EBPALPHA-DNA COMPLEX

Template:ABSTRACT PUBMED 12578822

About this Structure

1NWQ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis for DNA recognition by the basic region leucine zipper transcription factor CCAAT/enhancer-binding protein alpha., Miller M, Shuman JD, Sebastian T, Dauter Z, Johnson PF, J Biol Chem. 2003 Apr 25;278(17):15178-84. Epub 2003 Feb 10. PMID:12578822

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