Abstract:
: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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Monneau YR,Nelson CJ,Mackereth CDdoi
10.1007/s12104-011-9338-xsubject
Has Abstractpub_date
2012-10-01 00:00:00pages
123-6issue
2eissn
1874-2718issn
1874-270Xjournal_volume
6pub_type
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