Structural comparison of the active site channels in rodent and primate vascular adhesion protein-1

Eva Bligt-Lindén, R Arunachalam, Vimal Parkash, Tiina Salminen

    Research output: Contribution to journalArticleScientificpeer-review

    6 Citations (Scopus)


    In this study, we have made homology models of mouse, rat, and monkey vascular adhesion protein-1 (VAP-1) to reveal basis for the species-specific ligand recognition of VAP-1. Based on the structural comparisons, rodent VAP-1s have a narrower active site channel than primate VAP-1s. The variable residues in mouse and rat VAP-1, Phe447 from arm I and the polar residues from the first alpha-helix of the D3 domain together with C-terminal residues are likely to affect ligand recognition and binding.
    Original languageUndefined/Unknown
    Pages (from-to)947–950
    Number of pages4
    JournalJournal of Neural Transmission
    Publication statusPublished - 2013
    MoE publication typeA1 Journal article-refereed


    • AOC3
    • Human VAP-1
    • Rodent VAP-1
    • Structural comparison
    • Ligand recognition

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