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    AnglerFish: a webserver for defining the geometry of α-Helices in membrane proteins

    Colledge, Matthew and Wallace, Bonnie A. (2016) AnglerFish: a webserver for defining the geometry of α-Helices in membrane proteins. Bioinformatics , btw781. ISSN 1367-4803.

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    Abstract

    Summary: Integral membrane proteins that form helical pores and bundles constitute major drug targets, and many of their structures have been defined by crystallography and cryo-electron microscopy. The gating of channels and ligand binding of transporters generally involves changes in orientation of one or more the constituent helices in the structures. At present there is no standard easily- accessible means for defining the orientation of a helix in a membrane protein structure. AnglerFish is a web-based tool for parameterising the angles of transmembrane helices based on PDB coordinates, with the helical orientations defined by the angles “tilt” and “swing”. AnglerFish is particularly useful for defining changes in structure between different states, including both symmetric and asymmetric transitions, and can be used to quantitate differences between related structures or different subunits within the same structure.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 10 Jan 2017 13:32
    Last Modified: 04 Sep 2017 14:23
    URI: http://eprints.bbk.ac.uk/id/eprint/17906

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