STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER PROTEIN-1

The structure of a chromatin binding domain from mouse chromatin modif ier protein 1 (MoMOD1) was determined using nuclear magnetic resonance (NMR) spectroscopy. The protein consists of an N-terminal three-stran ded anti-parallel beta-sheet which folds against a C-terminal alpha-he lix. The structure reveals an unexpected homology to two archaebacteri al DNA binding proteins which are also involved in chromatin structure . Structural comparisons suggest that chrome domains, of which more th an 40 are now known, act as protein interaction moths and that the MoM OD1 protein acts as an adaptor mediating interactions between differen t proteins.