Cargando…
The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition
To maintain the integrity of the genome, multiple DNA repair systems exist to repair damaged DNA. Recognition of altered DNA, including bulky adducts, pyrimidine dimers and interstrand crosslinks (ICL), partially depends on proteins containing helix-hairpin-helix (HhH) domains. To understand how ICL...
Autores principales: | Wienk, Hans, Slootweg, Jack C., Speerstra, Sietske, Kaptein, Robert, Boelens, Rolf, Folkers, Gert E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711432/ https://www.ncbi.nlm.nih.gov/pubmed/23661679 http://dx.doi.org/10.1093/nar/gkt354 |
Ejemplares similares
-
Architecture and DNA Recognition Elements of the Fanconi Anemia FANCM-FAAP24 Complex
por: Coulthard, Rachel, et al.
Publicado: (2013) -
Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization
por: Tripsianes, Konstantinos, et al.
Publicado: (2007) -
Structural insights into the functions of the FANCM-FAAP24 complex in DNA repair
por: Yang, Hui, et al.
Publicado: (2013) -
Prolyl isomerization of FAAP20 catalyzed by PIN1 regulates the Fanconi anemia pathway
por: Wang, Jingming, et al.
Publicado: (2019) -
Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain
por: Wojtaszek, Jessica L., et al.
Publicado: (2014)