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Title: Structural and functional relationship of Pin1
Keywords: Pin1, isomerization, α1/β1 loop, model, melting temperature, selectivity
Issue Date: 13-Jun-2007
Citation: SONG PEI CHEE (2007-06-13). Structural and functional relationship of Pin1. ScholarBank@NUS Repository.
Abstract: Pin1 is a novel prolyl isomerase that specifically catalyzes cis/trans-isomerization of proline in the sequence of phosphorylated Ser/Thr-Pro in many mitotic proteins. We solved seven Pin1 mutants crystal structures and compared to the published wild-type structures. The I?1/I?1 loop of the mutants was in closed conformation although no sulphate or phosphate was recruited to the catalytic site, which contradicts to the previously proposed a??induced-fita?? model. Here, we proposed a a??two-step induced-fita?? model, in which substrate binding to the WW domain induces the opening of I?1/I?1 loop for the recruitment of second recognition motif to the catalytic site. This second binding in turn induces the closure of I?1/I?1 loop again, followed by substrate conformational change through cis-trans isomerization of proline thus to regulate substrate activity. In addition, the PPIase active site around Cys-113 and Met-130 could be a very rigid region to serve as a critical selectivity filter for substrate binding.
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