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Article

Conformational effects of a common codon 399 polymorphism on the BRCT1 domain of the XRCC1 protein.

The protein journal - 1 Dec 2007

Monaco Regina, Rosal Ramon, Dolan Michael A, Pincus Matthew R, Brandt-Rauf Paul W

Abstract excerpt

The X-ray cross-complementing-1 (XRCC1) protein functions as a scaffold that coordinates the activity of the cellular machinery involved in base excision repair (BER) of DNA damage. The BRCT1 domain of XRCC1 is responsible for interacting with several of the key components of the BER machinery, a...

Read the complete abstract on PubMed

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17899335
DOI: 10.1007/s10930-007-9095-y

Genes

XRCC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17899335-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Conformational effects of a common codon 399 polymorphism on the BRCT1 domain of the XRCC1 protein.PMID 17899335Read ↗

The region of XRCC1 which harbours the three most common nonsynonymous polymorphic variants, is essential for the scaffolding function of XRCC1.Semantic proximity Read ↗

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X-Ray Repair Cross Complementing Protein 1 in Base Excision RepairSemantic proximity Read ↗

Molecular dynamics simulations reveal R399Q mutation disrupts XRCC1-polβ interaction, potentially impairing DNA base excision repair pathway.Semantic proximity Read ↗

Molecular docking and molecular dynamics study on the effect of ERCC1 deleterious polymorphisms in ERCC1-XPF heterodimer.Semantic proximity Read ↗

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