Ball L J, Murzina N V, Broadhurst R W, Raine A R, Archer S J, Stott F J, Murzin A G, Singh P B, Domaille P J, Laue E D
Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, UK.
EMBO J. 1997 May 1;16(9):2473-81. doi: 10.1093/emboj/16.9.2473.
The structure of a chromatin binding domain from mouse chromatin modifier protein 1 (MoMOD1) was determined using nuclear magnetic resonance (NMR) spectroscopy. The protein consists of an N-terminal three-stranded anti-parallel beta-sheet which folds against a C-terminal alpha-helix. The structure reveals an unexpected homology to two archaebacterial DNA binding proteins which are also involved in chromatin structure. Structural comparisons suggest that chromo domains, of which more than 40 are now known, act as protein interaction motifs and that the MoMOD1 protein acts as an adaptor mediating interactions between different proteins.
利用核磁共振(NMR)光谱法确定了来自小鼠染色质修饰蛋白1(MoMOD1)的染色质结合结构域的结构。该蛋白由一个N端的三链反平行β折叠片层组成,其与一个C端的α螺旋折叠在一起。该结构揭示了与两种古细菌DNA结合蛋白意想不到的同源性,这两种蛋白也参与染色质结构。结构比较表明,现已发现40多种的染色体结构域作为蛋白质相互作用基序发挥作用,并且MoMOD1蛋白作为一种衔接子介导不同蛋白质之间的相互作用。