Monneau Yoan R, Nelson Christopher J, Mackereth Cameron D
Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33607 Pessac Cedex, France.
Biomol NMR Assign. 2012 Oct;6(2):123-6. doi: 10.1007/s12104-011-9338-x. Epub 2011 Sep 7.
Yeast Fpr4p belongs to the FK506-binding protein (FKBP) class of peptidyl proline isomerases (PPIases), and has been implicated in regulating the cis-trans conversion of proline residues within histone tails. Here we report the (1)H, (13)C and (15)N chemical shift assignments for the bacterially expressed C-terminal PPIase catalytic domain of Fpr4p. Prediction of secondary structure reveals similarity to domains from other members of the FKBP proline isomerases, including yeast Fpr1p and the prototypic PPIase region from human FKBP12.
酵母Fpr4p属于肽基脯氨酸异构酶（PPIase）的FK506结合蛋白（FKBP）类别，并且与调节组蛋白尾部脯氨酸残基的顺反异构化有关。在此，我们报道了细菌表达的Fpr4p的C端PPIase催化结构域的（1）H、（13）C和（15）N化学位移归属。二级结构预测显示其与FKBP脯氨酸异构酶其他成员的结构域相似，包括酵母Fpr1p和人FKBP12的典型PPIase区域。
