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• W1967710614 abstract "Abstract Symmetry plays significant roles in protein structure and function. Particularly, symmetric interfaces are known to act as switches for two‐state conformational change. Membrane proteins often undergo two‐state conformational change during the transport process of ion channels or the active/inactive transitions in receptors. Here, we provide the first comprehensive analyses of internal repeat symmetry in membrane proteins. We examined the known membrane protein structures and found that, remarkably, nearly half of them have internal repeat symmetry. Moreover, we found that the conserved cores of these internal repeats are positioned at the interface of symmetric units when they are mapped on structures. Because of the large sequence divergence that occurs between internal repeats, the inherent symmetry present in protein sequences often has only been detected after structure determination. We therefore developed a sensitive procedure to predict the internal repeat symmetry from sequence information and identified 4653 proteins that are likely to have internal repeat symmetry. Proteins 2008. © 2007 Wiley‐Liss, Inc." @default.
• W1967710614 created "2016-06-24" @default.
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• W1967710614 date "2007-10-11" @default.
• W1967710614 modified "2023-10-10" @default.
• W1967710614 title "Common occurrence of internal repeat symmetry in membrane proteins" @default.
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• W1967710614 doi "https://doi.org/10.1002/prot.21656" @default.
• W1967710614 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17932930" @default.
• W1967710614 hasPublicationYear "2007" @default.
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