Polypeptide chains with similar amino acid sequences but a distinctly different conformation: Bovine and porcine phospholipase A2

Bauke Dijkstra, WJ WEIJER, Rik K. Wierenga

    Research output: Contribution to journalLetterAcademicpeer-review

    18 Citations (Scopus)

    Abstract

    The primary structures of bovine and porcine pancreatic phospholipase A2 differ only by about 15%. Nevertheless, a 12 residue loop, with only one substitution (Val→Phe) has a quite different conformation, whereas the rest of the molecules have a very similar folding indeed. From this observation it is concluded that prediction of a 3-dimensional structure on the basis of sequence similarity of short segments alone might give erroneous results.
    Original languageEnglish
    Pages (from-to)25-27
    Number of pages3
    JournalFEBS Letters
    Volume164
    Issue number1
    DOIs
    Publication statusPublished - 1983

    Keywords

    • Sequence similarity
    • Phospholipase A2
    • Prediction of conformation
    • Amino acid sequence

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