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Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway.


ABSTRACT: Fanconi anemia is a cancer predisposition syndrome caused by defects in the repair of DNA interstrand cross-links (ICLs). Central to this pathway is the Fanconi anemia I-Fanconi anemia D2 (FANCI-FANCD2) (ID) complex, which is activated by DNA damage-induced phosphorylation and monoubiquitination. The 3.4 angstrom crystal structure of the ~300 kilodalton ID complex reveals that monoubiquitination and regulatory phosphorylation sites map to the I-D interface, suggesting that they occur on monomeric proteins or an opened-up complex and that they may serve to stabilize I-D heterodimerization. The 7.8 angstrom electron-density map of FANCI-DNA crystals and in vitro data show that each protein has binding sites for both single- and double-stranded DNA, suggesting that the ID complex recognizes DNA structures that result from the encounter of replication forks with an ICL.

SUBMITTER: Joo W 

PROVIDER: S-EPMC3310437 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway.

Joo Woo W   Xu Guozhou G   Persky Nicole S NS   Smogorzewska Agata A   Rudge Derek G DG   Buzovetsky Olga O   Elledge Stephen J SJ   Pavletich Nikola P NP  

Science (New York, N.Y.) 20110701 6040


Fanconi anemia is a cancer predisposition syndrome caused by defects in the repair of DNA interstrand cross-links (ICLs). Central to this pathway is the Fanconi anemia I-Fanconi anemia D2 (FANCI-FANCD2) (ID) complex, which is activated by DNA damage-induced phosphorylation and monoubiquitination. The 3.4 angstrom crystal structure of the ~300 kilodalton ID complex reveals that monoubiquitination and regulatory phosphorylation sites map to the I-D interface, suggesting that they occur on monomeri  ...[more]

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