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2IF5

Structure of the POZ domain of human LRF, a master regulator of oncogenesis

Summary for 2IF5
Entry DOI10.2210/pdb2if5/pdb
DescriptorZinc finger and BTB domain-containing protein 7A, PRASEODYMIUM ION (3 entities in total)
Functional Keywordspoz domain, btb domain, pok, proto oncogene, transcription factor, transcription
Biological sourceHomo sapiens (human)
Cellular locationNucleus (By similarity): O95365
Total number of polymer chains1
Total formula weight13362.36
Authors
Schubot, F.D.,Waugh, D.S.,Tropea, J. (deposition date: 2006-09-20, release date: 2006-11-21, Last modification date: 2023-08-30)
Primary citationSchubot, F.D.,Tropea, J.E.,Waugh, D.S.
Structure of the POZ domain of human LRF, a master regulator of oncogenesis.
Biochem.Biophys.Res.Commun., 351:1-6, 2006
Cited by
PubMed Abstract: The proto-oncogenic properties of the POK family of transcriptional repressors BCL6, PLZF, and LRF have been well established. These proteins utilize their amino-terminal POZ domains for multimerization and the recruitment of co-repressors. Because LRF represses the production of the tumor suppressor p19(Arf) (ARF), it is regarded as an attractive therapeutic target for the treatment of many types of cancer. The crystal structure of the LRF POZ domain reveals a high degree of structural conservation with the corresponding domains of BCL6 and PLZF. However, striking differences between the electrostatic properties of the BCL6 and LRF POZ domains suggest that if, like BCL6, LRF interacts with the co-repressor SMRT, it almost certainly uses a different mechanism to do so. These differences may also explain why LRF interacts with BCL6 but not with PLZF. Finally, the conservation of crystal packing contacts suggests the probable location of the interface that mediates LRF/BCL6 complex formation.
PubMed: 17052694
DOI: 10.1016/j.bbrc.2006.09.167
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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