2k1q | pdb_00002k1q

NMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently bound phenethylamide inhibitor

spinqualitylabelsall models 2k1q, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k1q is a 2 chain structure with sequence from 9hepc. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN NonStd Res: FE3, IBU, OBF Related: 1bt7, 1dwx Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed We present the first structure of a noncovalent inhibitor bound to the protease domain of hepatitis C virus NS3 protein (NS3p), solved by NMR. The inhibitor exploits interactions with the S' region of NS3p to form a long-lived complex, although the absence of negative charges strongly reduces the association rate. The inhibitor stabilizes the N-terminal domain of NS3p and the substrate-binding site, and correctly aligns catalytic His-Asp residues. These actions were previously attributed exclusively to the cofactor NS4A, which interacts with the N-terminal domain of the NS3p and functions as an activator in vivo. The structure of the inhibitor/NS3p complex is very similar to that of the NS3p-NS4A complex, showing that binding of the NS4A cofactor is not the only event leading to a stable active-site conformation. Binding of a noncovalent inhibitor exploiting the S' region stabilizes the hepatitis C virus NS3 protease conformation in the absence of cofactor.,Gallo M, Pennestri M, Bottomley MJ, Barbato G, Eliseo T, Paci M, Narjes F, De Francesco R, Summa V, Koch U, Bazzo R, Cicero DO J Mol Biol. 2009 Jan 30;385(4):1142-55. Epub 2008 Nov 24. PMID:19061898 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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