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Papers In Press, published online ahead of print September 28, 2005
NMR Based Structural Biology, Max-Planck Institute, Göttingen 37077
Corresponding Author: sabe{at}nmr.mpibpc.mpg.de
STAT proteins have the function of signaling from the cell membrane into the nucleus, where they regulate gene transcription. Latent mammalian STAT proteins can form dimers in the cytoplasm already before receptor-mediated activation by specific tyrosine phosphorylation. Here we describe the 3.21 Å crystal structure of an unphosphorylated STAT5a homodimer lacking the N-domain as well as the C-terminal transactivation domain. The overall structure of this fragment is very similar to phosphorylated STATs. However important differences exist in the dimerization mode. Whereas the interface between phosphorylated STATs is mediated by their SH2 domains, the unphosphorylated STAT5a fragment dimerizes in a completely different manner via interactions between their ß barrel and four-helix bundle domains. The STAT4 N-domain dimer can be docked onto this STAT5a core fragment dimer based on shape and charge complementarities. The separation of the dimeric arrangement, taking place upon activation and nuclear translocation of STAT5a, is demonstrated by FRET experiments in living cells.
J. Biol. Chem, 10.1074/jbc.M507682200
Submitted on July 15, 2005
Revised on September 26, 2005
Accepted on September 28, 2005
Structure of the unphosphorylated STAT5a dimer
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