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https://scholarbank.nus.edu.sg/handle/10635/23129
DC Field | Value | |
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dc.title | Structural and functional relationship of Pin1 | |
dc.contributor.author | SONG PEI CHEE | |
dc.date.accessioned | 2011-06-10T18:02:43Z | |
dc.date.available | 2011-06-10T18:02:43Z | |
dc.date.issued | 2007-06-13 | |
dc.identifier.citation | SONG PEI CHEE (2007-06-13). Structural and functional relationship of Pin1. ScholarBank@NUS Repository. | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/23129 | |
dc.description.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. | |
dc.language.iso | en | |
dc.subject | Pin1, isomerization, α1/β1 loop, model, melting temperature, selectivity | |
dc.type | Thesis | |
dc.contributor.department | BIOCHEMISTRY | |
dc.contributor.supervisor | TANG BOR LUEN | |
dc.contributor.supervisor | LIOU YIH-CHERNG | |
dc.description.degree | Master's | |
dc.description.degreeconferred | MASTER OF SCIENCE | |
dc.identifier.isiut | NOT_IN_WOS | |
Appears in Collections: | Master's Theses (Open) |
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File | Description | Size | Format | Access Settings | Version | |
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Thesis (Master of Science 2007, SONG PEI CHEE HT030439R).pdf | 7.36 MB | Adobe PDF | OPEN | None | View/Download |
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