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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...
Αποθηκεύτηκε σε:
| Τόπος έκδοσης: | J Biol Chem |
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| Κύριοι συγγραφείς: | , , , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
American Society for Biochemistry and Molecular Biology
2019
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| Θέματα: | |
| Διαθέσιμο Online: | 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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