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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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| Udgivet i: | J Biol Chem |
|---|---|
| Main Authors: | , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Biochemistry and Molecular Biology
2019
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| Fag: | |
| Online adgang: | 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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