6yd2 | pdb_00006yd2

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

spinqualitylabelsall models 6yd2, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yd2 is a 2 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: 00S, BVK, CA, CL, DMS, GGB, NA, PO4, TBG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FURIN_HUMAN Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif. Publication Abstract from PubMed 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. The Basicity Makes the Difference: Improved Canavanine-Derived Inhibitors of the Proprotein Convertase Furin.,Lam van TV, Heindl MR, Schlutt C, Bottcher-Friebertshauser E, Bartenschlager R, Klebe G, Brandstetter H, Dahms SO, Steinmetzer T ACS Med Chem Lett. 2021 Feb 9;12(3):426-432. doi: 10.1021/acsmedchemlett.0c00651., eCollection 2021 Mar 11. PMID:33732412 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Furin

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