Insights into the molecular features of the von Hippel–Lindau-like protein

Giovanni Minervini, Federica Quaglia, Francesco Tabaro, Silvio C.E. Tosatto

    Research output: Contribution to journalArticleScientificpeer-review

    2 Citations (Scopus)


    We present an in silico characterization of the von Hippel–Lindau-like protein (VLP), the only known human paralog of the von Hippel–Lindau tumor suppressor protein (pVHL). Phylogenetic investigation showed VLP to be mostly conserved in upper mammals and specifically expressed in brain and testis. Structural analysis and molecular dynamics simulations show VLP to be very similar to pVHL three-dimensional organization and binding dynamics. In particular, conservation of elements at the protein interfaces suggests VLP to be a functional pVHL homolog potentially possessing multiple functions beyond HIF-1α-dependent binding activity. Our findings show that VLP may share at least seven interactors with pVHL, suggesting novel functional roles for this understudied human protein. These may occur at precise hypoxia levels where functional overlap with pVHL may permit a finer modulation of pVHL functions.

    Original languageEnglish
    Pages (from-to)1461-1474
    Number of pages14
    JournalAmino Acids
    Issue number10-12
    Publication statusPublished - 2019
    Publication typeA1 Journal article-refereed


    • Bioinformatics
    • Cancer
    • Hereditary neoplastic syndrome
    • Von Hippel–Lindau disease

    Publication forum classification

    • Publication forum level 1

    ASJC Scopus subject areas

    • Biochemistry
    • Clinical Biochemistry
    • Organic Chemistry


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