1ci6
From Proteopedia
(New page: 200px<br /> <applet load="1ci6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ci6, resolution 2.6Å" /> '''TRANSCRIPTION FACTOR...) |
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caption="1ci6, resolution 2.6Å" /> | caption="1ci6, resolution 2.6Å" /> | ||
'''TRANSCRIPTION FACTOR ATF4-C/EBP BETA BZIP HETERODIMER'''<br /> | '''TRANSCRIPTION FACTOR ATF4-C/EBP BETA BZIP HETERODIMER'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CI6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with FE and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CI6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:35:51 2008'' |
Revision as of 13:35, 15 February 2008
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TRANSCRIPTION FACTOR ATF4-C/EBP BETA BZIP HETERODIMER
Overview
The crystal structure of the heterodimer formed by the basic leucine, zipper (bZIP) domains of activating transcription factor-4 (ATF4) and, CCAAT box/enhancer-binding protein beta (C/EBP beta), from two different, bZIP transcription factor families, has been determined and refined to 2.6, A. The structure shows that the heterodimer forms an asymmetric, coiled-coil. Even in the absence of DNA, the basic region of ATF4 forms a, continuous alpha-helix, but the basic region of C/EBP beta is disordered., Proteolysis, electrophoretic mobility shift assay, circular dichroism, and, NMR analyses indicated that (i) the bZIP domain of ATF4 is a disordered, monomer and forms a homodimer upon binding to the DNA target; (ii) the, bZIP domain of ATF4 forms a heterodimer with the bZIP domain of C/EBP beta, that binds the cAMP response element, but not CCAAT box DNA, with high, affinity; and (iii) the basic region of ATF4 has a higher alpha-helical, propensity than that of C/EBP beta. These results suggest that the degree, of ordering of the basic region and the fork and the dimerization, properties of the leucine zipper combine to distinguish the structurally, similar bZIP domains of ATF4 and C/EBP beta with respect to DNA target, sequence. This study provides insight into the mechanism by which dimeric, bZIP transcription factors discriminate between closely related but, distinct DNA targets.
About this Structure
1CI6 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA., Podust LM, Krezel AM, Kim Y, J Biol Chem. 2001 Jan 5;276(1):505-13. PMID:11018027
Page seeded by OCA on Fri Feb 15 15:35:51 2008
Categories: Homo sapiens | Mus musculus | Protein complex | Kim, Y. | Podust, L.M. | BME | FE | Bzip | Transcription factor
