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Article

Effects of naturally occurring charged mutations on the structure, stability, and binding of the Pin1 WW domain.

Biochemical and biophysical research communications - 27 May 2017

Qiao Xiaoya, Liu Ying, Luo Liting, Chen Lei, Zhao Caixian, Ai Xuanjun

Abstract excerpt

Pin1 is a peptidyl-prolyl cis-trans isomerase, whose WW domain specifically recognizes the pSer/Thr-Pro motif. Pin1 is involved in multiple phosphorylation events that regulate the activities of various substrates, and Pin1 deregulation has been reported in various diseases, including cancer and Alzheimer's disease. The WW domain of Pin1 has been used as a small model protein to investigate the folding mechanisms...

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Identifiers

PMID: 28431929
DOI: 10.1016/j.bbrc.2017.04.093

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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