Neighboring phosphoSer‐Pro motifs in the undefined domain of IRAK 1 impart bivalent advantage for Pin1 binding
Abstract
The peptidyl prolyl isomerase Pin1 has two domains that are considered to be its binding (WW) and catalytic (PPIase) domains, both of which interact with phosphorylated Ser/Thr-Pro motifs. This shared specificity might influence substrate selection, as many known Pin1 substrates have multiple sequentially close phosphoSer/Thr-Pro motifs, including the protein interleukin-1 receptor-associated kinase-1 (IRAK1). The IRAK1 undefined domain (UD)...
Paper Details
Title
Neighboring phosphoSer‐Pro motifs in the undefined domain of IRAK 1 impart bivalent advantage for Pin1 binding
Published Date
Nov 20, 2016
Journal
Volume
283
Issue
24
Pages
4528 - 4548
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