Asn78 and His81 form a destabilizing locus within the Max HLH‐LZ homodimer

FEBS Letters

Weiss, Anthony S¹  Tchan, Michel C¹ 

[1] Department of Biochemistry, University of Sydney, Sydney, NSW 2006, Australia

关键词: Coiled-coil;    Helix-loop-helix;    Leucine zipper;    Max;    c-Myc;    Protein–protein interaction;    HLH;    helix-loop-helix;    LZ;    leucine zipper;    CD;    circular dichroism;   

DOI  :  10.1016/S0014-5793(01)03166-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The human Max protein lies at the center of the Myc/Max/Mad family of transcription factors. Its role at the center of this regulatory network is dependent on the helix-loop-helix leucine zipper (HLH-LZ) dimerization domain. The Max LZ contains three residues that deviate from the pattern of hydrophobic amino acids normally present at the interface of LZ dimers: Asn⁷⁸, His⁸¹ and Asn⁹². In contrast to interfacial Asn residues in other LZ proteins, we have shown that Asn⁹² does not act to destabilize the homodimer. Here we describe thermal denaturation experiments performed on Asn⁷⁸ and His⁸¹ mutants demonstrating that these residues are involved in actively destabilizing the Max homodimer.

【 授权许可】

Unknown