The crystal structure of human cyclin H

被引:31
作者
Andersen, G [1 ]
Poterszman, A [1 ]
Egly, JM [1 ]
Moras, D [1 ]
Thierry, JC [1 ]
机构
[1] UNIV STRASBOURG 1, INSERM, CNRS, INST GENET & BIOL MOL & CELLULAIRE, F-67404 ILLKIRCH GRAFFENSTADEN, FRANCE
关键词
human; cyclin; cell cycle; TFIIH; transcription factor; X-ray structure;
D O I
10.1016/S0014-5793(96)01143-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of human cyclin H has been solved at 2.6 Angstrom 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.
引用
收藏
页码:65 / 69
页数:5
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