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  • Molecular modelling of prohibitin domains

    Author(s)
    Winter, Anja
    Kamarainen, Outi
    Hofmann, Andreas
    Griffith University Author(s)
    Hofmann, Andreas
    Winter, Anja
    Year published
    2007
    Metadata
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    Abstract
    Prohibitins comprise a family of highly conserved ubiquitous eukaryotic proteins that mainly localize to the mitochondria. They have been implicated in important cellular processes such as cellular signaling and transcriptional control, apoptosis, cellular senescence, and mitochondrial biogenesis. Using molecular modeling techniques, we have generated structural models of human prohibitions BAP32 and BAP37 which have previously been shown to exist as large ring-like oligomers in the membrane-bound state. The middle domain of prohibitins is evolutionary conserved in the family of SPFH (PHB) domain proteins. Based on the known ...
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    Prohibitins comprise a family of highly conserved ubiquitous eukaryotic proteins that mainly localize to the mitochondria. They have been implicated in important cellular processes such as cellular signaling and transcriptional control, apoptosis, cellular senescence, and mitochondrial biogenesis. Using molecular modeling techniques, we have generated structural models of human prohibitions BAP32 and BAP37 which have previously been shown to exist as large ring-like oligomers in the membrane-bound state. The middle domain of prohibitins is evolutionary conserved in the family of SPFH (PHB) domain proteins. Based on the known structure of flotillin-2, another member of the SPFH domain family, we have generated homology models for BAP32 and BAP37, and elucidated the implications for formation of high molecular weight oligomers. A model for the dimeric building block of BAP32:BAP37 for such assemblies was generated and its stability scrutinized by molecular dynamics simulations. The model of BAP32 was also analyzed as to potential ligand binding sites and the previously identified ligand melanogenin was docked into a membrane-proximal cavity. The results are discussed in the context of prohibitin interactions with mitochondrial AAA-proteases and we suggest two possible interaction interfaces between the BAP32:BAP37 building block and the protease.
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    Journal Title
    Proteins: Structure, Function, and Bioinformatics
    Volume
    68
    Issue
    1
    Publisher URI
    http://www3.interscience.wiley.com
    DOI
    https://doi.org/10.1002/prot.21355
    Copyright Statement
    © 2007 John Wiley & Sons, Ltd. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please refer to the journal link for access to the definitive, published version or contact the author for more information.
    Subject
    Mathematical sciences
    Biological sciences
    Information and computing sciences
    Publication URI
    http://hdl.handle.net/10072/18849
    Collection
    • Journal articles

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