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

Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.

Nucleic acids research - 1 Jan 2006

Plotz Guido, Welsch Christoph, Giron-Monzon Luis, Friedhoff Peter, Albrecht Mario, Piiper Albrecht, Biondi Ricardo M, Lengauer Thomas, Zeuzem Stefan, Raedle Jochen

Abstract excerpt

MutLalpha, a heterodimer of MLH1 and PMS2, plays a central role in human DNA mismatch repair. It interacts ATP-dependently with the mismatch detector MutSalpha and assembles and controls further repair enzymes. We tested if the interaction of MutLalpha with DNA-bound MutSalpha is impaired by cancer-associated mutations in MLH1, and identified one mutation (Ala128Pro) which abolished interaction as well as...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Adenosine Triphosphatases

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

Share to Carrier Proteins

Share to DNA Mismatch Repair

Share to Escherichia coli Proteins

Share to MutL Protein Homolog 1

Share to MutL Proteins

Share to MutS Homolog 2 Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 17135187
DOI: 10.1093/nar/gkl944
PMCID: PMC1747184

Genes

MLH1
PMS2

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

Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.PMID 17135187Read ↗

Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair.Semantic proximity Read ↗

A conserved motif in the disordered linker of human MLH1 is vital for DNA mismatch repair and its function is diminished by a cancer family mutation.Semantic proximity Read ↗

Disruption of protein-protein interaction hotspots in the C-terminal domain of MLH1 confers mismatch repair deficiency.Semantic proximity Read ↗

Disentangling the mutational effects on protein stability and interaction of human MLH1Semantic proximity Read ↗

Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations.Semantic proximity Read ↗

Disentangling the mutational effects on protein stability and interaction of human MLH1Semantic proximity Read ↗

Intrinsically disordered regions regulate both catalytic and non-catalytic activities of the MutLα mismatch repair complex.Semantic proximity Read ↗

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch.Semantic proximity Read ↗

Contribution of Human Mlh1 and Pms2 ATPase Activities to DNA Mismatch RepairSemantic proximity Read ↗

Characterization of a highly conserved binding site of Mlh1 required for exonuclease I-dependent mismatch repair.Semantic proximity Read ↗

Characterization of the DNA mismatch repair proteins MutS and MutL in a hypermutator Acinetobacter baumannii.Semantic proximity Read ↗

Mispair-bound human MutS–MutL complex triggers DNA incisions and activates mismatch repairSemantic proximity Read ↗

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