6YD2

X-ray structure of furin in complex with the canavanine-based inhibitor 4-aminomethyl-phenylacetyl-canavanine-Tle-Arg-Amba

This is a non-PDB format compatible entry.

Summary for 6YD2

• Entry DOI: 10.2210/pdb6yd2/pdb
• Descriptor: Furin, 4-aminomethyl-phenylacetyl-canavanine-Tle-Arg-Amba, CALCIUM ION, ... (8 entities in total)
• Functional Keywords: protease, inhibitor, complex, canavanine, hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 53578.20

Authors

Dahms, S.O. (deposition date: 2020-03-20, release date: 2021-02-17, Last modification date: 2024-01-31)

Primary citation

Lam van, T.V.,Heindl, M.R.,Schlutt, C.,Bottcher-Friebertshauser, E.,Bartenschlager, R.,Klebe, G.,Brandstetter, H.,Dahms, S.O.,Steinmetzer, T.
The Basicity Makes the Difference: Improved Canavanine-Derived Inhibitors of the Proprotein Convertase Furin.
Acs Med.Chem.Lett., 12:426-432, 2021

PubMed Abstract: Furin activates numerous viral glycoproteins, and its inhibition prevents virus replication and spread. Through the replacement of arginine by the less basic canavanine, new inhibitors targeting furin in the trans-Golgi network were developed. These inhibitors exert potent antiviral activity in cell culture with much lower toxicity than arginine-derived analogues, most likely due to their reduced protonation in the blood circulation. Thus, despite its important physiological functions, furin might be a suitable antiviral drug target.

PubMed: 33732412
DOI: 10.1021/acsmedchemlett.0c00651

Experimental method

X-RAY DIFFRACTION (1.8 Å)