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Article

Structural Insight into the Mechanism of TFIIH Recognition by the Acidic String of the Nucleotide Excision Repair Factor XPC.

Structure (London, England : 1993) - 6 Oct 2015

Okuda Masahiko, Kinoshita Minoru, Kakumu Erina, Sugasawa Kaoru, Nishimura Yoshifumi

Abstract excerpt

In global genome repair (GGR), XPC detects damaged nucleotides and recruits TFIIH complex. The small acidic region of XPC binds to the pleckstrin homology (PH) domain of TFIIH subunit p62; however, the recognition mechanism remains elusive. Here, we use nuclear magnetic resonance to present the tertiary structure of XPC bound to the PH domain. The XPC acidic region forms a long string stabilized by insertion of...

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Identifiers

PMID: 26278177
DOI: 10.1016/j.str.2015.07.009

Genes

XPC

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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.

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