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Article

Dynamics of Aromatic Side Chains in the Active Site of FKBP12.

Biochemistry - 10 Jan 2017

Weininger Ulrich, Modig Kristofer, Geitner Anne-Juliane, Schmidpeter Philipp A M, Koch Johanna R, Akke Mikael

Abstract excerpt

FKBP12, a small human enzyme, aids protein folding by catalyzing cis-trans isomerization of peptidyl-prolyl bonds, and is involved in cell signaling pathways, calcium regulation, and the immune response. The underlying molecular mechanisms are not fully understood, but it is well-known that aromatic residues in the active site and neighboring loops are important for substrate binding and catalysis. Here we report...

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Identifiers

PMID: 27936610
DOI: 10.1021/acs.biochem.6b01157

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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