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

Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.

Nucleic acids research - 1 Jan 2014

Miętus Michał, Nowak Elżbieta, Jaciuk Marcin, Kustosz Paweł, Studnicka Justyna, Nowotny Marcin

Abstract excerpt

Rad2/XPG belongs to the flap nuclease family and is responsible for a key step of the eukaryotic nucleotide excision DNA repair (NER) pathway. To elucidate the mechanism of DNA binding by Rad2/XPG, we solved crystal structures of the catalytic core of Rad2 in complex with a substrate. Rad2 utilizes three structural modules for recognition of the double-stranded portion of DNA substrate, particularly a...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endodeoxyribonucleases

Share to Endonucleases

Share to Exodeoxyribonucleases

Share to Flap Endonucleases

Share to Nuclear Proteins

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 25120270
DOI: 10.1093/nar/gku729
PMCID: PMC4176360

Genes

EXO1
FEN1

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

Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.PMID 25120270Read ↗

Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations.Semantic proximity Read ↗

XPA: A key scaffold for human nucleotide excision repair.Semantic proximity Read ↗

Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG.Semantic proximity Read ↗

Structural insights into 5' flap DNA unwinding and incision by the human FAN1 dimer.Semantic proximity Read ↗

Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair.Semantic proximity Read ↗

Structural basis for DNA break recognition by ARTD2/PARP2Semantic proximity Read ↗

Significance of the dissociation of Dna2 by flap endonuclease 1 to Okazaki fragment processing in Saccharomyces cerevisiae.Semantic proximity Read ↗

Structural and functional analyses of an archaeal XPF/Rad1/Mus81 nuclease: asymmetric DNA binding and cleavage mechanisms.Semantic proximity Read ↗

Does the XPA–FEN1 Interaction Concern to Nucleotide Excision Repair or Beyond?Semantic proximity Read ↗

Mechanism of BCDX2-mediated RAD51 nucleation on short ssDNA stretches and fork DNA.Semantic proximity Read ↗

BRCA2 C-terminal clamp restructures RAD51 dimers to bind B-DNA for replication fork stability.Semantic proximity Read ↗

The secondary-structured DNA-binding activity of Dna2 endonuclease/helicase is critical to cell growth under replication stress.Semantic proximity Read ↗

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