Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization
YR Monneau, H Soufari, CJ Nelson… - Journal of Biological …, 2013 - ASBMB
The FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases (PPIases) is
characterized by a common catalytic domain that binds to the inhibitors FK506 and
rapamycin. As one of four FKBPs within the yeast Saccharomyces cerevisiae, Fpr4 has been
described as a histone chaperone, and is in addition implicated in epigenetic function in part
due to its mediation of cis-trans conversion of proline residues within histone tails. To better
understand the molecular details of this activity, we have determined the solution structure of …
characterized by a common catalytic domain that binds to the inhibitors FK506 and
rapamycin. As one of four FKBPs within the yeast Saccharomyces cerevisiae, Fpr4 has been
described as a histone chaperone, and is in addition implicated in epigenetic function in part
due to its mediation of cis-trans conversion of proline residues within histone tails. To better
understand the molecular details of this activity, we have determined the solution structure of …
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