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

Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease.

Nature structural biology - 1 Sept 2001

Batra R, Khayat R, Tong L

Abstract excerpt

Biochemical studies indicate that dimerization is required for the catalytic activity of herpesvirus proteases, whereas structural studies show a complete active site in each monomer, away from the dimer interface. Here we report kinetic, biophysical and crystallographic characterizations of structure-based mutants in the dimer interface of human cytomegalovirus (HCMV) protease. Such mutations can produce a...

Read the complete abstract on PubMed

Topics

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

Share to Anions
Share to Centrifugation
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytomegalovirus

Share to Dimerization

Share to Fluorescence

Share to Protein Structure, Quaternary

Share to Serine Endopeptidases

Source

Identifiers

PMID: 11524687
DOI: 10.1038/nsb0901-810

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease.PMID 11524687Read ↗

Cooperativity and communication between the active sites of the dimeric SARS-CoV-2 main protease.Semantic proximity Read ↗

Mechanism for controlling the monomer-dimer conversion of SARS coronavirus main protease.Semantic proximity Read ↗

Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties.Semantic proximity Read ↗

A naturally occurring G11S mutation in the 3C-like protease from the SARS-CoV-2 virus dramatically weakens the dimer interface.Semantic proximity Read ↗

Mutation of Asn28 disrupts the dimerization and enzymatic activity of SARS 3CL(pro) .Semantic proximity Read ↗

Folded monomer of HIV-1 protease.Semantic proximity Read ↗

The Herpesvirus Proteases as Targets for Antiviral ChemotherapySemantic proximity Read ↗

Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations.Semantic proximity Read ↗

The mechanism by which P250L mutation impairs flavivirus-NS1 dimerization: an investigation based on molecular dynamics simulations.Semantic proximity Read ↗

Molecular Interplay between the Dimer Interface and the Substrate-Binding Site of Human Peptidylarginine Deiminase 4.Semantic proximity Read ↗

Mutation of Glu-166 blocks the substrate-induced dimerization of SARS coronavirus main protease.Semantic proximity Read ↗

Dimerization of bacterial diaminopimelate epimerase is essential for catalysis.Semantic proximity Read ↗

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