1NFA

HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10 STRUCTURES

Summary for 1NFA

• Entry DOI: 10.2210/pdb1nfa/pdb
• Descriptor: HUMAN TRANSCRIPTION FACTOR NFATC1 (1 entity in total)
• Functional Keywords: nfat, transcription regulation, rel-homology fold, activates cytokine transcription
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O95644
• Total number of polymer chains: 1
• Total formula weight: 19985.85

Authors

Wolfe, S.A.,Zhou, P.,Dotsch, V.,Chen, L.,You, A.,Ho, S.N.,Crabtree, G.R.,Wagner, G.,Verdine, G.L. (deposition date: 1997-01-18, release date: 1997-04-01, Last modification date: 2024-05-22)

Primary citation

Wolfe, S.A.,Zhou, P.,Dotsch, V.,Chen, L.,You, A.,Ho, S.N.,Crabtree, G.R.,Wagner, G.,Verdine, G.L.
Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc.
Nature, 385:172-176, 1997

PubMed Abstract: Transcription factors of the NFAT family regulate the production of effector proteins that coordinate the immune response. The immunosuppressive drugs FK506 and cyclosporin A (CsA) act by blocking a Ca2+-mediated signalling pathway leading to NFAT. Although FK506 and CsA have enabled human organs to be transplanted routinely, the toxic side-effects of these drugs limit their usage. This toxicity might be absent in antagonists that target NFAT directly. As a first step in the structure-based search for NFAT antagonists, we now report the identification and solution structure of a 20K domain of NFATc (NFATc-DBD) that is both necessary and sufficient to bind DNA and activate transcription cooperatively. Although the overall fold of the NFATc DNA-binding domain is related to that of NF-kappaB p50 (refs 2, 3), the two proteins use significantly different strategies for DNA recognition. On the basis of these results, we present a model for the cooperative complex formed between NFAT and the mitogenic transcription factor AP-1 on the interleukin-2 enhancer.

PubMed: 8990122
DOI: 10.1038/385172a0

Experimental method

SOLUTION NMR