dc.contributor.author |
Beaulieu, Marie-Eve |
dc.contributor.author |
Castillo, Francisco |
dc.contributor.author |
Soucek, Laura |
dc.date |
2020 |
dc.date.accessioned |
2022-10-31T00:12:52Z |
dc.date.available |
2022-10-31T00:12:52Z |
dc.date.issued |
2022-10-31 |
dc.identifier |
https://ddd.uab.cat/record/252573 |
dc.identifier |
urn:10.3390/cells9041038 |
dc.identifier |
urn:oai:ddd.uab.cat:252573 |
dc.identifier |
urn:pmcid:PMC7226237 |
dc.identifier |
urn:pmc-uid:7226237 |
dc.identifier |
urn:pmid:32331235 |
dc.identifier |
urn:oai:pubmedcentral.nih.gov:7226237 |
dc.identifier |
urn:articleid:20734409v9n4p1038 |
dc.identifier.uri |
http://hdl.handle.net/2072/525234 |
dc.format |
application/pdf |
dc.language |
eng |
dc.publisher |
|
dc.relation |
European Commission 872212 |
dc.relation |
European Commission 617473 |
dc.relation |
Cells ; Vol. 9, Issue 4 (April 2020), art. 1038 |
dc.rights |
open access |
dc.rights |
Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. |
dc.rights |
https://creativecommons.org/licenses/by/4.0/ |
dc.subject |
Myc |
dc.subject |
MAX |
dc.subject |
Protein-protein interactions |
dc.subject |
Protein-dna interactions |
dc.subject |
Intrinsically disordered proteins |
dc.subject |
Biophysics |
dc.subject |
Drug discovery |
dc.title |
Structural and biophysical insights into the function of the intrinsically disordered Myc oncoprotein |
dc.type |
Article |
dc.description.abstract |
Myc is a transcription factor driving growth and proliferation of cells and involved in the majority of human tumors. Despite a huge body of literature on this critical oncogene, our understanding of the exact molecular determinants and mechanisms that underlie its function is still surprisingly limited. Indubitably though, its crucial and non-redundant role in cancer biology makes it an attractive target. However, achieving successful clinical Myc inhibition has proven challenging so far, as this nuclear protein is an intrinsically disordered polypeptide devoid of any classical ligand binding pockets. Indeed, Myc only adopts a (partially) folded structure in some contexts and upon interacting with some protein partners, for instance when dimerizing with MAX to bind DNA. Here, we review the cumulative knowledge on Myc structure and biophysics and discuss the implications for its biological function and the development of improved Myc inhibitors. We focus this biophysical walkthrough mainly on the basic region helix-loop-helix leucine zipper motif (bHLHLZ), as it has been the principal target for inhibitory approaches so far. |