Evolution and Medical Significance of LU Domain-Containing Proteins
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Evolution and Medical Significance of LU Domain-Containing Proteins. / Leth, Julie Maja; Leth-Espensen, Katrine Zinck; Kristensen, Kristian Kølby; Kumari, Anni; Lund Winther, Anne-Marie; Young, Stephen G; Ploug, Michael.
In: International Journal of Molecular Sciences, Vol. 20, No. 11, 2019, p. 1-20.Research output: Contribution to journal › Review › Research › peer-review
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TY - JOUR
T1 - Evolution and Medical Significance of LU Domain-Containing Proteins
AU - Leth, Julie Maja
AU - Leth-Espensen, Katrine Zinck
AU - Kristensen, Kristian Kølby
AU - Kumari, Anni
AU - Lund Winther, Anne-Marie
AU - Young, Stephen G
AU - Ploug, Michael
PY - 2019
Y1 - 2019
N2 - 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.
AB - 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.
U2 - 10.3390/ijms20112760
DO - 10.3390/ijms20112760
M3 - Review
C2 - 31195646
VL - 20
SP - 1
EP - 20
JO - International Journal of Molecular Sciences (CD-ROM)
JF - International Journal of Molecular Sciences (CD-ROM)
SN - 1424-6783
IS - 11
ER -
ID: 225390878