Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis.

Journal of virology - 1 Jan 2007

Sweeney Trevor R, Roqué-Rosell Núria, Birtley James R, Leatherbarrow Robin J, Curry Stephen

Abstract excerpt

The 3C protease (3C(pro)) from foot-and-mouth disease virus (FMDV), the causative agent of a widespread and economically devastating disease of domestic livestock, is a potential target for antiviral drug design. We have determined the structure of a new crystal form of FMDV 3C(pro), a chymotrypsin-like cysteine protease, which reveals features that are important for catalytic activity. In particular, we show...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Structure, Tertiary

Share to Substrate Specificity

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 17065215
DOI: 10.1128/JVI.01587-06
PMCID: PMC1797255

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis.PMID 17065215Read ↗

Identification of the active-site residues of the 3C proteinase of foot-and-mouth disease virus.Semantic proximity Read ↗

Mutational analysis of the active centre of coronavirus 3C-like proteases.Semantic proximity Read ↗

3-Chymotrypsin-like Protease (3CLpro): Validation as a Molecular Target, Proposal of a Novel Catalytic Mechanism, and Inhibitors in Preclinical and Clinical TrialsSemantic proximity Read ↗

Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.Semantic proximity Read ↗

Structure of Senecavirus A 3C Protease Revealed the Cleavage Pattern of 3C Protease in PicornavirusesSemantic proximity Read ↗

Foot-and-Mouth Disease Virus 3C Protease Cleaves NEMO To Impair Innate Immune SignalingSemantic proximity Read ↗

Analysis of putative active site residues of the poliovirus 3C protease.Semantic proximity Read ↗

Insights into polyprotein processing and RNA-protein interactions in foot-and-mouth disease virus genome replicationSemantic proximity Read ↗

Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host CellsSemantic proximity Read ↗

Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase.Semantic proximity Read ↗

Mutational analysis of the putative substrate-binding site of 3C proteinase of coxsackievirus B3.Semantic proximity Read ↗

Norovirus Protease Structure and Antivirals Development.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.