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Article

Structural rationale for the coupled binding and unfolding of the c-Myc oncoprotein by small molecules.

Chemistry & biology - 24 Nov 2008

Follis Ariele Viacava, Hammoudeh Dalia I, Wang Huabo, Prochownik Edward V, Metallo Steven J

Abstract excerpt

The basic-helix-loop-helix-leucine-zipper domains of the c-Myc oncoprotein and its obligate partner Max are intrinsically disordered (ID) monomers that undergo coupled folding and binding upon heterodimerization. We have identified the binding sites and determined the structural means by which two unrelated small molecules, 10058-F4 and 10074-G5, bind c-Myc and stabilize the ID monomer over the highly ordered...

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Source

Identifiers

PMID: 19022175
DOI: 10.1016/j.chembiol.2008.09.011

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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