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Article

The helix located between the two domains of a mip-like peptidyl-prolyl cis-trans isomerase is crucial for its structure, stability, and protein folding ability.

Biochemistry - 9 Oct 2012

Jana Biswanath, Sau Subrata

Abstract excerpt

FKBP22, a PPIase (peptidyl-prolyl cis-trans isomerase) produced by Escherichia coli, binds FK506 and rapamycin (both immunosuppressive drugs), shares significant homology with the Mip-like virulence factors, and has been thought to carry a long α-helix (namely α3) between its two domains. To understand whether the length of helix α3 plays any role in the structure, function, and stability of FKBP22-like proteins,...

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Identifiers

PMID: 22989269
DOI: 10.1021/bi300720g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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