2if5

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[[Image:2if5.gif|left|200px]]<br />
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[[Image:2if5.gif|left|200px]]<br /><applet load="2if5" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2if5" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2if5, resolution 2.00&Aring;" />
caption="2if5, resolution 2.00&Aring;" />
'''Structure of the POZ domain of human LRF, a master regulator of oncogenesis'''<br />
'''Structure of the POZ domain of human LRF, a master regulator of oncogenesis'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2IF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IF5 OCA].
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2IF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PR:'>PR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IF5 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Schubot, F.D.]]
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[[Category: Schubot, F D.]]
[[Category: Tropea, J.]]
[[Category: Tropea, J.]]
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[[Category: Waugh, D.S.]]
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[[Category: Waugh, D S.]]
[[Category: PR]]
[[Category: PR]]
[[Category: btb domain]]
[[Category: btb domain]]
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:44:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:59 2008''

Revision as of 15:52, 21 February 2008


2if5, resolution 2.00Å

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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 with as ligand. 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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