Structure of the FANCI-FANCD2 Complex: Insights into the Fanconi Anemia DNA Repair Pathway
Copyright policy )Structure of the FANCI-FANCD2 Complex: Insights into the Fanconi Anemia DNA Repair Pathway
The ID complex reveals how phosphorylation and ubiquitination could influence its stability and DNA-binding functions.
- Rockefeller University United States
- Harvard University United States
- Howard Hughes Medical Institute United States
- Brigham and Women's Faulkner Hospital United States
- Memorial Sloan Kettering Cancer Center United States
Models, Molecular, Protein Folding, Binding Sites, DNA Repair, Protein Conformation, Fanconi Anemia Complementation Group D2 Protein, Molecular Sequence Data, DNA, Single-Stranded, DNA, Crystallography, X-Ray, Fanconi Anemia Complementation Group Proteins, Protein Structure, Secondary, Protein Structure, Tertiary, Mice, Fanconi Anemia, Animals, Amino Acid Sequence, Phosphorylation, Hydrophobic and Hydrophilic Interactions, Protein Binding
Models, Molecular, Protein Folding, Binding Sites, DNA Repair, Protein Conformation, Fanconi Anemia Complementation Group D2 Protein, Molecular Sequence Data, DNA, Single-Stranded, DNA, Crystallography, X-Ray, Fanconi Anemia Complementation Group Proteins, Protein Structure, Secondary, Protein Structure, Tertiary, Mice, Fanconi Anemia, Animals, Amino Acid Sequence, Phosphorylation, Hydrophobic and Hydrophilic Interactions, Protein Binding
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