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5I4Z

Structure of apo OmoMYC

Summary for 5I4Z
Entry DOI10.2210/pdb5i4z/pdb
DescriptorMyc proto-oncogene protein, GLYCEROL, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsleucine zipper, transcription factor, tumor suppressor, e-box, transcription
Biological sourceHomo sapiens (Human)
Cellular locationNucleus, nucleoplasm : P01106
Total number of polymer chains2
Total formula weight28532.93
Authors
Koelmel, W.,Jung, L.A.,Kuper, J.,Eilers, M.,Kisker, C. (deposition date: 2016-02-13, release date: 2016-10-26, Last modification date: 2024-11-20)
Primary citationJung, L.A.,Gebhardt, A.,Koelmel, W.,Ade, C.P.,Walz, S.,Kuper, J.,von Eyss, B.,Letschert, S.,Redel, C.,d'Artista, L.,Biankin, A.,Zender, L.,Sauer, M.,Wolf, E.,Evan, G.,Kisker, C.,Eilers, M.
OmoMYC blunts promoter invasion by oncogenic MYC to inhibit gene expression characteristic of MYC-dependent tumors.
Oncogene, 36:1911-1924, 2017
Cited by
PubMed Abstract: MYC genes have both essential roles during normal development and exert oncogenic functions during tumorigenesis. Expression of a dominant-negative allele of MYC, termed OmoMYC, can induce rapid tumor regression in mouse models with little toxicity for normal tissues. How OmoMYC discriminates between physiological and oncogenic functions of MYC is unclear. We have solved the crystal structure of OmoMYC and show that it forms a stable homodimer and as such recognizes DNA in the same manner as the MYC/MAX heterodimer. OmoMYC attenuates both MYC-dependent activation and repression by competing with MYC/MAX for binding to chromatin, effectively lowering MYC/MAX occupancy at its cognate binding sites. OmoMYC causes the largest decreases in promoter occupancy and changes in expression on genes that are invaded by oncogenic MYC levels. A signature of OmoMYC-regulated genes defines subgroups with high MYC levels in multiple tumor entities and identifies novel targets for the eradication of MYC-driven tumors.
PubMed: 27748763
DOI: 10.1038/onc.2016.354
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

229183

数据于2024-12-18公开中

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