Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond?

The urokinase receptor (uPAR) is a founding member of a small protein family with multiple Ly6/uPAR (LU) domains. The motif defining these LU domains contains five plesiotypic disulfide bonds stabilizing its prototypical three-fingered fold having three protruding loops. Notwithstanding the detailed...

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Gorde:
Xehetasun bibliografikoak
Argitaratua izan da:J Biol Chem
Egile Nagusiak: Leth, Julie M., Mertens, Haydyn D. T., Leth-Espensen, Katrine Zinck, Jørgensen, Thomas J. D., Ploug, Michael
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: American Society for Biochemistry and Molecular Biology 2019
Gaiak:
Protein Structure and Folding
Sarrera elektronikoa:https://ncbi.nlm.nih.gov/pmc/articles/PMC6509485/
https://ncbi.nlm.nih.gov/pubmed/30894413
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.007847
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