TY - JOUR
T1 - Structural aspects of interactions within the Myc/Max/Mad network
AU - Nair, S. K.
AU - Burley, S. K.
PY - 2006
Y1 - 2006
N2 - Recently determined structures of a number of Myc family proteins have provided significant insights into the molecular nature of complex assembly and DNA binding. These structures illuminate the details of specific interactions that govern the assembly of nucleoprotein complexes and, in doing so, raise more questions regarding Myc biology. In this review, we focus on the lessons provided by these structures toward understanding (1) interactions that govern transcriptional repression by Mad via the Sin3 pathway, (2) homodimerization of Max, (3) heterodimerizalion of Myc-Max and Mad-Max, and (4) DNA recognition by each of the Max-Max, Myc-Max, and Mad-Max dimers.
AB - Recently determined structures of a number of Myc family proteins have provided significant insights into the molecular nature of complex assembly and DNA binding. These structures illuminate the details of specific interactions that govern the assembly of nucleoprotein complexes and, in doing so, raise more questions regarding Myc biology. In this review, we focus on the lessons provided by these structures toward understanding (1) interactions that govern transcriptional repression by Mad via the Sin3 pathway, (2) homodimerization of Max, (3) heterodimerizalion of Myc-Max and Mad-Max, and (4) DNA recognition by each of the Max-Max, Myc-Max, and Mad-Max dimers.
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U2 - 10.1007/3-540-32952-8_5
DO - 10.1007/3-540-32952-8_5
M3 - Review article
C2 - 16620027
AN - SCOPUS:33144486890
SN - 0070-217X
VL - 302
SP - 123
EP - 143
JO - Current Topics in Microbiology and Immunology
JF - Current Topics in Microbiology and Immunology
ER -