Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p.

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 Assign

authors

Monneau YR,Nelson CJ,Mackereth CD

doi

10.1007/s12104-011-9338-x

subject

Has Abstract

pub_date

2012-10-01 00:00:00

pages

123-6

issue

2

eissn

1874-2718

issn

1874-270X

journal_volume

6

pub_type

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