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Evolution and Medical Significance of LU Domain-Containing Proteins

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Proteins containing Ly6/uPAR (LU) domains exhibit very diverse biological functions and have broad taxonomic distributions in eukaryotes. In general, they adopt a characteristic three-fingered folding topology with three long loops projecting from a disulfide-rich globular core. The majority of the members of this protein domain family contain only a single LU domain, which can be secreted, glycolipid anchored, or constitute the extracellular ligand binding domain of type-I membrane proteins. Nonetheless, a few proteins contain multiple LU domains, for example, the urokinase receptor uPAR, C4.4A, and Haldisin. In the current review, we will discuss evolutionary aspects of this protein domain family with special emphasis on variations in their consensus disulfide bond patterns. Furthermore, we will present selected cases where missense mutations in LU domain-containing proteins leads to dysfunctional proteins that are causally linked to genesis of human disease.

Original languageEnglish
Article number2760
JournalInternational Journal of Molecular Sciences
Volume20
Issue number11
ISSN1661-6596
DOIs
Publication statusPublished - 1 Jun 2019

    Research areas

  • GPIHBP1, Ly6/uPAR domains, Plesiotypic disulfide bonds, Protein domain, Protein evolution, Protein module, Snake venom α-neurotoxins, UPAR

ID: 57488387