Dimerization, but not phosphothreonine binding, is conserved between the forkhead‐associated domains of Drosophila MU2 and human MDC1
Copyright policy )Dimerization, but not phosphothreonine binding, is conserved between the forkhead‐associated domains of Drosophila MU2 and human MDC1
MU2 and MU2 bind by molecular sieving (View interaction)
- China Agricultural University China (People's Republic of)
- University of Minnesota System United States
- National Institute of Biological Sciences, Beijing China (People's Republic of)
- University of Minnesota United States
Models, Molecular, Molecular Sequence Data, Cell Cycle Proteins, DNA damage response, Crystallography, X-Ray, MDC1, Animals, Drosophila Proteins, Humans, Forkhead-associated domain, Amino Acid Sequence, Protein Structure, Quaternary, Conserved Sequence, X-ray crystallography, Adaptor Proteins, Signal Transducing, Binding Sites, Sequence Homology, Amino Acid, Nuclear Proteins, Recombinant Proteins, Protein Structure, Tertiary, DNA-Binding Proteins, Phosphothreonine, Trans-Activators, Molecular evolution, Dimerization
Models, Molecular, Molecular Sequence Data, Cell Cycle Proteins, DNA damage response, Crystallography, X-Ray, MDC1, Animals, Drosophila Proteins, Humans, Forkhead-associated domain, Amino Acid Sequence, Protein Structure, Quaternary, Conserved Sequence, X-ray crystallography, Adaptor Proteins, Signal Transducing, Binding Sites, Sequence Homology, Amino Acid, Nuclear Proteins, Recombinant Proteins, Protein Structure, Tertiary, DNA-Binding Proteins, Phosphothreonine, Trans-Activators, Molecular evolution, Dimerization
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