dc.contributor | Vall d'Hebron Barcelona Hospital Campus |
dc.contributor.author | Castillo, Francisco |
dc.contributor.author | Beaulieu, Marie-Eve |
dc.contributor.author | Soucek, Laura |
dc.date.accessioned | 2021-09-01T11:04:56Z |
dc.date.available | 2021-09-01T11:04:56Z |
dc.date.issued | 2020-04-22 |
dc.identifier.citation | Beaulieu ME, Castillo F, Soucek L. Structural and Biophysical Insights into the Function of the Intrinsically Disordered Myc Oncoprotein. Cells. 2020 Apr 22;9(4):1038. |
dc.identifier.issn | 2073-4409 |
dc.identifier.uri | https://hdl.handle.net/11351/6252 |
dc.description | Myc; Drug discovery; Protein–DNA interactions |
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. |
dc.language.iso | eng |
dc.publisher | MDPI |
dc.relation.ispartofseries | Cells;9(4) |
dc.rights | Attribution 4.0 International |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ |
dc.source | Scientia |
dc.subject | Medicaments - Desenvolupament |
dc.subject | ADN - Interaccions de les proteïnes |
dc.subject | Oncogens |
dc.subject.mesh | Proto-Oncogene Proteins c-myc |
dc.subject.mesh | Intrinsically Disordered Proteins |
dc.subject.mesh | Drug Evaluation, Preclinical |
dc.title | Structural and Biophysical Insights into the Function of the Intrinsically Disordered Myc Oncoprotein |
dc.type | info:eu-repo/semantics/article |
dc.identifier.doi | 10.3390/cells9041038 |
dc.subject.decs | proteínas protooncogénicas c-myc |
dc.subject.decs | proteínas intrínsecamente desestructuradas |
dc.subject.decs | evaluación preclínica de medicamentos |
dc.relation.publishversion | https://www.mdpi.com/2073-4409/9/4/1038 |
dc.type.version | info:eu-repo/semantics/publishedVersion |
dc.audience | Professionals |
dc.contributor.organismes | Institut Català de la Salut |
dc.contributor.authoraffiliation | [Beaulieu ME, Castillo F] Peptomyc, Barcelona, Spain. [Soucek L] Peptomyc, Barcelona, Spain. Vall d’Hebron Institute of Oncology (VHIO), Barcelona, Spain. Institució Catalana de Recerca i Estudis Avançats (ICREA), Barcelona, Spain. Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Spain |
dc.identifier.pmid | 32331235 |
dc.identifier.wos | 000535559500249 |
dc.relation.projectid | info:eu-repo/grantAgreement/EC/H2020/872212 |
dc.relation.projectid | info:eu-repo/grantAgreement/EC/H2020/617473 |
dc.rights.accessrights | info:eu-repo/semantics/openAccess |