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Both the helix-loop-helix and the leucine zipper motifs of c-Myc contribute to its dimerization specificity with Max.

Abstract：

:The oncoprotein c-Myc contains two dimerization motifs- the helix-loop-helix (HLH) and the leucine zipper (LZ) - through which c-Myc specifically dimerizes with Max. We substituted regions of the c-Myc HLH and LZ motifs with the corresponding regions of structurally related proteins that do not interact with Max. Specific association of c-Myc with Max was dictated by helices 1 and 2 of the HLH motif and by the LZ. Within helix 2, residues 6 and 7 were important determinants of dimerization specificity. c-Myc and Max proteins with three amino acids inserted between their HLH and LZ motifs interacted efficiently, suggesting that the spacing between the motifs can be varied. Furthermore, alignment of the motifs at the primary sequence level was not obligatory, since Max with the three amino acid insertion could interact with wild-type c-Myc. These findings are consistent with our recently proposed model for the architecture of HLH/LZ domains.

journal_name

Oncogene

journal_title

Oncogene

authors

Davis LJ,Halazonetis TD

subject

Has Abstract

pub_date

1993-01-01 00:00:00

pages

125-32

issue

1

eissn

0950-9232

issn

1476-5594

journal_volume

8

pub_type

杂志文章

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