CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA

Structure of NFAT Bound to DNA as a Monomer

NFAT1 Monomeric Binding Site, Plus Strand

NFAT1 Monomeric Binding Site, Minus Strand

Nuclear factor of activated T-cells, cytoplasmic 2

T cell transcription factor NFAT1, NFAT pre-existing subunit, NF-ATp

VPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFY
QVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESS
GRIVSLQTASNPIECSQRSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQ
PNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV

sodium cacodylate, magnesium chloride, peg 3000, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 289K

Structure Of The DNA Binding Domains Of Nfat, Fos and Jun Bound To DNA

The plus strand of the NFAT1 monomeric binding site was chemically synthesized

The minus strand of the NFAT1 monomeric binding site was chemically synthesized

Starting model is the structure of the DNA binding domains of nfat, fos and jun bound to DNA without RHR-N bound to b-form dsDNA

The biological unit is a single protein polymer of the NFAT1 RHR in complex with a double stranded piece of DNA of 13 base pairs with a 2 base overhang at the 5' end. There are 4 such biological units in the asymmetric unit.

BETA BARREL, PROTEIN-DNA COMPLEX, DOUBLE HELIX, BINARY, MONOMER, PSEUDO-CONTINUOUS, TRANSCRIPTION-DNA COMPLEX

PLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQ
VHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSG
RIVSLQTASNPIECSQRSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQP
NMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV