Summary information and primary citation

PDB-id
5g35; DSSR-derived features in text and JSON formats
Class
cell cycle
Method
X-ray (2.0 Å)
Summary
Structure of rad14 in complex with acetylaminopyren-c8-guanine containing DNA
Reference
Schneider S, Simon N, Ebert C (2016): "Structural Basis for Bulky Adduct DNA Lesion Recognition by the Nucleotide Excision Repair Protein Rad14." Chemistry, 22, 10782. doi: 10.1002/CHEM.201602438.
Abstract
Heterocyclic aromatic amines react with purine bases and result in bulky DNA adducts which cause mutations. Such structurally diverse lesions are substrates for the nucleotide excision repair (NER). It is thought that the NER machinery recognises distorted DNA conformations, involving the xeroderma pigmentosum group A and C (XPA, XPC) proteins as a scaffold between the DNA substrate and several other NER proteins. Here we present the synthesis of DNA containing the polycyclic aromatic amine C8-guanine lesions acetylaminophenyl, acetylaminonaphthyl, acetylaminoanthryl and acetylaminopyrenyl as well as their crystal structures in in complex with the yeast XPA homologue Rad14. This work further substantiates the indirect lesion detection mechanism employed by the NER system to recognise destabilised and deformable DNA structures.

Cartoon-block schematics in six views (download the tarball)

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