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    Folding Pathways for Initiator and Effector Procaspases from Computer Simulations

    Access Status
    Fulltext not available
    Authors
    Piana, Stefano
    Taylor, Zoe
    Rothlisberger, U.
    Date
    2005
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Piana, Stefano and Taylor, Zoe and Rothlisberger, Ursula. 2005. Folding Pathways for Initiator and Effector Procaspases from Computer Simulations. Proteins: Structure, Function, and Bioinformatics 59: 765-772.
    Source Title
    Proteins: Structure, Function, and Bioinformatics
    DOI
    10.1002/prot.20451
    Faculty
    Department of Applied Chemistry
    Division of Engineering, Science and Computing
    Faculty of Science
    Remarks

    Copyright 2005 John Wiley & Sons, Ltd.

    Please refer to the publisher for the definitive published version.

    URI
    http://hdl.handle.net/20.500.11937/35535
    Collection
    • Curtin Research Publications
    Abstract

    The folding pathways of procaspases 3, 7, and 8 have been studied using a Go-like Hamiltonian and molecular dynamics simulations coupled with a parallel tempering scheme. The folding pathways and the overall structures of procaspases 3 and 7 are similar, and are characterized by monomeric as well as dimeric folding intermediates in agreement with the available structural and thermochemical data. The folding pathway of procaspase 8, on the other hand, is characterized by a larger population of monomers and partially folded dimer intermediates, and only a relatively small population of folded dimer species. The most stable structure predicted for procaspase 8 is a dimer,in which the position of the linker is remarkably different from the one observed in procaspases 3 and 7, leading to the fact that all the contacts that stabilize the active site are essentially formed. This novel and unexpected structure provides a rationale for the observed activity of the procaspase 8 dimer, and thus could be highly relevant for the initiation of FAS-mediated apoptosis. Proteins 2005;59:765-772.(c)2005 Wiley-Liss, Inc.

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