Publication Abstract from PubMed
The crystal structure of human cyclin H has been solved at 2.6 A resolution by the MIR method and refined to an R-factor of 23.1%. The core of the molecule consists of two helical repeats adopting the canonical cyclin fold already observed in the structures of cyclin A [Brown et al. (1995) Structure 3, 1235-1247; Jeffrey et al. (1995) Nature 376, 313-320; Russo et al. (1996) Nature 382, 325-331] and TFIIB [Nikoilov et al. (1995) Nature 377, 119-128]. The N-terminal and C-terminal residues form a new domain built on two long helices interacting essentially with the first repeat of the molecule.
The crystal structure of human cyclin H.,Andersen G, Poterszman A, Egly JM, Moras D, Thierry JC FEBS Lett. 1996 Nov 11;397(1):65-9. PMID:8941715[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
