2if5
From Proteopedia
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|PDB= 2if5 |SIZE=350|CAPTION= <scene name='initialview01'>2if5</scene>, resolution 2.00Å | |PDB= 2if5 |SIZE=350|CAPTION= <scene name='initialview01'>2if5</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PR:PRASEODYMIUM ION'>PR</scene> | + | |LIGAND= <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ZBTB7A, FBI1, LRF, ZBTB7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ZBTB7A, FBI1, LRF, ZBTB7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2if5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2if5 OCA], [http://www.ebi.ac.uk/pdbsum/2if5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2if5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Tropea, J.]] | [[Category: Tropea, J.]] | ||
[[Category: Waugh, D S.]] | [[Category: Waugh, D S.]] | ||
| - | [[Category: PR]] | ||
[[Category: btb domain]] | [[Category: btb domain]] | ||
[[Category: pok]] | [[Category: pok]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:43:27 2008'' |
Revision as of 00:43, 31 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ZBTB7A, FBI1, LRF, ZBTB7 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the POZ domain of human LRF, a master regulator of oncogenesis
Overview
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.
About this Structure
2IF5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the POZ domain of human LRF, a master regulator of oncogenesis., Schubot FD, Tropea JE, Waugh DS, Biochem Biophys Res Commun. 2006 Dec 8;351(1):1-6. Epub 2006 Oct 9. PMID:17052694
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