BIROn - Birkbeck Institutional Research Online

    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.

    17906.pdf - Published Version of Record
    Available under License Creative Commons Attribution.

    Download (125kB) | Preview


    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.


    Item Type: Article
    School: School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 10 Jan 2017 13:32
    Last Modified: 09 Jun 2021 12:16


    Activity Overview

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item