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2K1Q

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

Summary for 2K1Q
Entry DOI10.2210/pdb2k1q/pdb
Related1bt7 1dwx
DescriptorNS3 PROTEASE, PHENETHYLAMIDE, ZINC ION (3 entities in total)
Functional Keywordsserine protease, ns3, hepatitis c virus, non covalent inhibitor, envelope protein, helicase, hydrolase, nucleotide-binding, rna replication, transmembrane, viral protein
Biological sourceHepatitis C virus
Total number of polymer chains2
Total formula weight20363.04
Authors
Eliseo, T.,Gallo, M.,Pennestri, M.,Bazzo, R.,Cicero, D.O. (deposition date: 2008-03-13, release date: 2009-02-03, Last modification date: 2023-11-15)
Primary citationGallo, M.,Pennestri, M.,Bottomley, M.J.,Barbato, G.,Eliseo, T.,Paci, M.,Narjes, F.,De Francesco, R.,Summa, V.,Koch, U.,Bazzo, R.,Cicero, D.O.
Binding of a noncovalent inhibitor exploiting the S' region stabilizes the hepatitis C virus NS3 protease conformation in the absence of cofactor.
J.Mol.Biol., 385:1142-1155, 2009
Cited by
PubMed Abstract: 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.
PubMed: 19061898
DOI: 10.1016/j.jmb.2008.11.017
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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