We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Cyclin
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
== 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. Two 5 α-helix cyclin boxes are shown.<ref>PMID:09433129</ref> | + | All cyclins have an all-α helix fold and share an identical ca. 100 residue domain called 'cyclin box' which binds CDK. <scene name='44/442748/Cv/3'>Two 5 α-helix cyclin boxes are shown</scene>.<ref>PMID:09433129</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 13:04, 21 December 2015
| |||||||||||
3D Structures of Cyclin
Updated on 21-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
- ↑ Noble ME, Endicott JA, Brown NR, Johnson LN. The cyclin box fold: protein recognition in cell-cycle and transcription control. Trends Biochem Sci. 1997 Dec;22(12):482-7. PMID:9433129
