1a02: Difference between revisions

Revision as of 15:41, 30 June 2008

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File:1a02.png

Template:STRUCTURE 1a02

STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNASTRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA

Template:ABSTRACT PUBMED 9510247

About this StructureAbout this Structure

1A02 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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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-'''STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA'''
+===STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9510247}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9510247 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9510247}}
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