Core-binding factor

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<StructureSection load='1h9d' size='340' side='right' caption='Human CBFα runt domain (grey and pink) complex with CBFβ heterodimerization domain (green and yellow) and DNA (PDB code [[1h9d]])' scene=''>
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<StructureSection load='' size='340' side='right' caption='Human CBFα runt domain (magenta) complex with CBFβ heterodimerization domain (green) and DNA (PDB code [[1h9d]])' scene='70/708082/Cv/1'>
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'''Core-binding factor''' (CBF) is a heterodimeric transcription factor which is composed of α chain which binds DNA and a regulatory β chain. CBF binds to various enhancers and promoters including murine leukemia virus and polyomavirus enhancer. CBF α contains a DNA-binding runt domain (residues 50-177).
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== Function ==
== Function ==
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'''Core-binding factor''' (CBF) is a heterodimeric transcription factor which is composed of <scene name='70/708082/Cv/2'>α chain which binds DNA and a regulatory β chain</scene>. CBF binds to various enhancers and promoters including murine leukemia virus and polyomavirus enhancer. <ref>PMID:11276260</ref>
== Disease ==
== Disease ==
Mutations in CBF β are implicated in breast cancer. Rearrangements of CBF α and β genes are implicated in acute myeloid leukemia.
Mutations in CBF β are implicated in breast cancer. Rearrangements of CBF α and β genes are implicated in acute myeloid leukemia.
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== Relevance ==
 
== Structural highlights ==
== Structural highlights ==
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CBF α contains a DNA-binding runt domain (residues 50-177).
</StructureSection>
</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
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*Core-binding factor α
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*Core-binding factor α subunit
**[[1ean]], [[1ljm]] – hCBFα runt domain - human<br />
**[[1ean]], [[1ljm]] – hCBFα runt domain - human<br />
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**[[1cmo]] – hCBFα runt domain (mutant) - NMR<br />
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**[[1cmo]], [[2n7b]] – hCBFα runt domain (mutant) - NMR<br />
**[[1co1]] – hCBFα runt domain - NMR<br />
**[[1co1]] – hCBFα runt domain - NMR<br />
**[[1eao]], [[1eaq]], [[2j6w]] – mCBFα runt domain (mutant) - mouse<br />
**[[1eao]], [[1eaq]], [[2j6w]] – mCBFα runt domain (mutant) - mouse<br />
**[[1hjc]] – mCBFα runt domain + DNA <br />
**[[1hjc]] – mCBFα runt domain + DNA <br />
**[[1hjb]] – mCBFα runt domain + hEBP β + DNA<br />
**[[1hjb]] – mCBFα runt domain + hEBP β + DNA<br />
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**[[4l0y]], [[4l0z]], [[4l18]], [[4wu1]] – mCBFα runt domain + hETS1 + DNA<br />
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**[[4l0y]], [[4l0z]], [[4l18]], [[3wu1]] – mCBFα runt domain + hETS1 + DNA<br />
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*Core-binding factor β subunit
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**[[4n9f]] – hCBFb + cullin-5 + elongin-B + virion infectivity factor<br />
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**[[6p59]] – hCBFb + elongin-B + elongin-C + virion infectivity factor<br />
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**[[6nil]] – hCBFb + A3F complex + virion infectivity factor – Cryo EM<br />
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**[[8e40]], [[8h0i]], [[8j62]] – hCBFb + APOBEC + virion infectivity factor + RNA – Cryo EM<br />
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**[[8cx0]], [[8cx1]], [[8cx2]] – hCBFb + elongin-B + elongin-C + APOBEC + virion infectivity factor + RNA – Cryo EM<br />
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**[[8fvi]] – hCBFb + APOBEC + virion infectivity factor + cullin 5 + RNA – Cryo EM<br />
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**[[8fvj]] – hCBFb + elongin-B + elongin-C + virion infectivity factor + cullin 5 – Cryo EM<br />
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**[[8szk]] – hCBFb + elongin-B + elongin-C + virion infectivity factor + cullin 5 + RNA – Cryo EM<br />
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**[[6vg2]], [[6vg8]], [[6vgd]], [[6vge]], [[6vgg]] – hCBFb + Runx2 + FLI1 + DNA<br />
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**[[1ilf]] – mCBFb<br />
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*Core-binding factor α+β
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*Core-binding factor α+β subunits
**[[1e50]] – hCBFα runt domain + hCBFβ heterodimerization domain<br />
**[[1e50]] – hCBFα runt domain + hCBFβ heterodimerization domain<br />
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== References ==
== References ==
<references/>
<references/>
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[[Category:Topic Page]]

Current revision

Human CBFα runt domain (magenta) complex with CBFβ heterodimerization domain (green) and DNA (PDB code 1h9d)

Drag the structure with the mouse to rotate

3D Structures of core-binding factor

Updated on 09-February-2025


References

  1. ↑ Bravo J, Li Z, Speck NA, Warren AJ. The leukemia-associated AML1 (Runx1)--CBF beta complex functions as a DNA-induced molecular clamp. Nat Struct Biol. 2001 Apr;8(4):371-8. PMID:11276260 doi:http://dx.doi.org/10.1038/86264

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Michal Harel, Joel L. Sussman, Alexander Berchansky

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