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The crystal structure of human cyclin H
Author(s) -
Andersen G.,
Poterszman A.,
Egly J.M.,
Moras D.,
Thierry J.-C.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01143-x
Subject(s) - crystal structure , cyclin a , chemistry , molecule , stereochemistry , cyclin , crystallography , biochemistry , gene , cell cycle , organic chemistry
The crystal structure of human cyclin H has been solved at 2.6 Å 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.