3OYP

HCV NS3/4A in complex with ligand 3

Summary for 3OYP

• Entry DOI: 10.2210/pdb3oyp/pdb
• Related PRD ID: PRD_000823
• Descriptor: Serine protease NS3, Non-structural protein 4A, Peptidomimetic inhibitor, ... (5 entities in total)
• Functional Keywords: serine protease, ns3, ns4a, hepatitis c virus, protease inhibition, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Hepatitis C virus (isolate Japanese) (HCV); More
• Cellular location: Core protein p21: Host endoplasmic reticulum membrane ; Single-pass membrane protein . Core protein p19: Virion . Envelope glycoprotein E1: Virion membrane ; Single-pass type I membrane protein . Envelope glycoprotein E2: Virion membrane ; Single-pass type I membrane protein . p7: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Protease NS2-3: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. RNA-directed RNA polymerase: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein : P26662 P26662
• Total number of polymer chains: 6
• Total formula weight: 44355.28

Authors

Hagel, M.,Niu, D.,St.Martin, T.,Sheets, M.P.,Qiao, L.,Bernard, H.,Karp, R.M.,Zhu, Z.,Labenski, M.T.,Chaturvedi, P.C.,Nacht, M.,Westlin, W.F.,Petter, R.C.,Singh, J. (deposition date: 2010-09-23, release date: 2010-12-01, Last modification date: 2023-11-15)

Primary citation

Hagel, M.,Niu, D.,St.Martin, T.,Sheets, M.P.,Qiao, L.,Bernard, H.,Karp, R.M.,Zhu, Z.,Labenski, M.T.,Chaturvedi, P.,Nacht, M.,Westlin, W.F.,Petter, R.C.,Singh, J.
Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine.
Nat.Chem.Biol., 7:22-24, 2011

PubMed Abstract: Designing selective inhibitors of proteases has proven problematic, in part because pharmacophores that confer potency exploit the conserved catalytic apparatus. We developed a fundamentally different approach by designing irreversible inhibitors that target noncatalytic cysteines that are structurally unique to a target in a protein family. We have successfully applied this approach to the important therapeutic target HCV protease, which has broad implications for the design of other selective protease inhibitors.

PubMed: 21113170
DOI: 10.1038/nchembio.492

Experimental method

X-RAY DIFFRACTION (2.76 Å)