A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn

V. S. Ananthanarayanan, K. V. Soman, C. Ramakrishnan

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    Abstract

    A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a β-turn is seen in several synthetic peptides and has been suggested to be the conformational requirement for proline hydroxylation in nascent procollagen. Using a simple algorithm for detecting secondary structures, we have analysed crystal structure data on 40 globular proteins and have found eight examples of the collagen-helix + β-turn supersecondary structure in 15 proteins that contain the collagen-like helical segments.

    Original languageEnglish (US)
    Pages (from-to)705-709
    Number of pages5
    JournalJournal of Molecular Biology
    Volume198
    Issue number4
    DOIs
    StatePublished - Dec 20 1987

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    ASJC Scopus subject areas

    • Structural Biology
    • Molecular Biology

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