1a02
From Proteopedia
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| - | [[Image:1a02.gif|left|200px]]<br /> | + | [[Image:1a02.gif|left|200px]]<br /><applet load="1a02" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a02" size=" | + | |
caption="1a02, resolution 2.700Å" /> | caption="1a02, resolution 2.700Å" /> | ||
'''STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA'''<br /> | '''STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The nuclear factor of activated T cells (NFAT) and the AP-1 heterodimer, Fos-Jun, cooperatively bind a composite DNA site and synergistically | + | The nuclear factor of activated T cells (NFAT) and the AP-1 heterodimer, Fos-Jun, cooperatively bind a composite DNA site and synergistically activate the expression of many immune-response genes. A 2.7-A-resolution crystal structure of the DNA-binding domains of NFAT, Fos and Jun, in a quaternary complex with a DNA fragment containing the distal antigen-receptor response element from the interleukin-2 gene promoter, shows an extended interface between NFAT and AP-1, facilitated by the bending of Fos and DNA. The tight association of the three proteins on DNA creates a continuous groove for the recognition of 15 base pairs. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A02 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1A02 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1A02 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Glover, J | + | [[Category: Glover, J N.M.]] |
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
| - | [[Category: Hogan, P | + | [[Category: Hogan, P G.]] |
[[Category: Rao, A.]] | [[Category: Rao, A.]] | ||
[[Category: ap-1]] | [[Category: ap-1]] | ||
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[[Category: transcription synergy]] | [[Category: transcription synergy]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:21 2008'' |
Revision as of 09:39, 21 February 2008
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STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA
Contents |
Overview
The nuclear factor of activated T cells (NFAT) and the AP-1 heterodimer, Fos-Jun, cooperatively bind a composite DNA site and synergistically activate the expression of many immune-response genes. A 2.7-A-resolution crystal structure of the DNA-binding domains of NFAT, Fos and Jun, in a quaternary complex with a DNA fragment containing the distal antigen-receptor response element from the interleukin-2 gene promoter, shows an extended interface between NFAT and AP-1, facilitated by the bending of Fos and DNA. The tight association of the three proteins on DNA creates a continuous groove for the recognition of 15 base pairs.
Disease
Known diseases associated with this structure: Autoimmune polyglandular disease, type I OMIM:[607358], Sveinsson choreoretinal atrophy OMIM:[189967]
About this Structure
1A02 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA., Chen L, Glover JN, Hogan PG, Rao A, Harrison SC, Nature. 1998 Mar 5;392(6671):42-8. PMID:9510247
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