Evolution and Medical Significance of LU Domain-Containing Proteins

Research output: Contribution to journal › Review › Research › peer-review

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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

Harvard

Leth, JM, Leth-Espensen, KZ, Kristensen, KK, Kumari, A, Lund Winther, A-M, Young, SG & Ploug, M 2019, 'Evolution and Medical Significance of LU Domain-Containing Proteins', International Journal of Molecular Sciences, vol. 20, no. 11, pp. 1-20. https://doi.org/10.3390/ijms20112760

APA

Leth, J. M., Leth-Espensen, K. Z., Kristensen, K. K., Kumari, A., Lund Winther, A-M., Young, S. G., & Ploug, M. (2019). Evolution and Medical Significance of LU Domain-Containing Proteins. International Journal of Molecular Sciences, 20(11), 1-20. https://doi.org/10.3390/ijms20112760

Vancouver

Leth JM, Leth-Espensen KZ, Kristensen KK, Kumari A, Lund Winther A-M, Young SG et al. Evolution and Medical Significance of LU Domain-Containing Proteins. International Journal of Molecular Sciences. 2019;20(11):1-20. https://doi.org/10.3390/ijms20112760

Author

Leth, Julie Maja ; Leth-Espensen, Katrine Zinck ; Kristensen, Kristian Kølby ; Kumari, Anni ; Lund Winther, Anne-Marie ; Young, Stephen G ; Ploug, Michael. / Evolution and Medical Significance of LU Domain-Containing Proteins. In: International Journal of Molecular Sciences. 2019 ; Vol. 20, No. 11. pp. 1-20.

Bibtex

@article{e7f268e3e3644e568c916bb5b2cc463e,
title = "Evolution and Medical Significance of LU Domain-Containing Proteins",
abstract = "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.",
author = "Leth, {Julie Maja} and Leth-Espensen, {Katrine Zinck} and Kristensen, {Kristian K{\o}lby} and Anni Kumari and {Lund Winther}, Anne-Marie and Young, {Stephen G} and Michael Ploug",
year = "2019",
doi = "10.3390/ijms20112760",
language = "English",
volume = "20",
pages = "1--20",
journal = "International Journal of Molecular Sciences (CD-ROM)",
issn = "1424-6783",
publisher = "M D P I AG",
number = "11",

}

RIS

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