Lei Jin1, 5, Piotr Sliz1, 5, Lin Chen1, 3, Fernando Macián2, 4, Anjana Rao2, Patrick G Hogan2
& Stephen C Harrison11
Department of Biological Chemistry and Molecular Pharmacology and Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
2
Center for Blood Research, Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02215, USA.
3
Present address: Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, Colorado 80309, USA.
4
Present address: Department of Pathology, 1300 Morris Park Avenue, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
5
These authors contributed equally to this work.
Correspondence should be addressed to Stephen C Harrison harrison@crystal.harvard.edu
B-like DNA site
B. Binding studies with a form of the NFAT1 RHR defective in the dimer contact show loss of cooperativity and demonstrate that the same interaction is present in solution. The structure we have determined may correspond to a functional NFAT binding mode at palindromic sites of genes induced during the anergic response to weak TCR signaling.
B element
