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Cyclin
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='3blh' size='350' side='right' caption='Cyclin | + | <StructureSection load='3blh' size='350' side='right' caption='Cyclin T1 (green) complex with CDK9 (grey) and TRIS (PDB entry [[3blh]])' scene=''> |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | All cyclins have an all-α helix fold and share an identical ca. 100 residue domain called 'cyclin box' which binds CDK. | + | All cyclins have an all-α helix fold and share an identical ca. 100 residue domain called 'cyclin box' which binds CDK. Two 5 α-helix cyclin boxes are shown. |
</StructureSection> | </StructureSection> | ||
Revision as of 10:13, 16 December 2015
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3D Structures of Cyclin
Updated on 16-December-2015
References
- ↑ Galderisi U, Jori FP, Giordano A. Cell cycle regulation and neural differentiation. Oncogene. 2003 Aug 11;22(33):5208-19. PMID:12910258 doi:http://dx.doi.org/10.1038/sj.onc.1206558
