A Structural Basis for the Biochemical Behavior of Activation-induced Deoxycytidine Deaminase Class-switch Recombination-defective Hyper-IgM-2 Mutants*

@article{Mu2012ASB,
  title={A Structural Basis for the Biochemical Behavior of Activation-induced Deoxycytidine Deaminase Class-switch Recombination-defective Hyper-IgM-2 Mutants*},
  author={Yunxiang Mu and Courtney Prochnow and P. Pham and Xiaojiang S. Chen and M. Goodman},
  journal={The Journal of Biological Chemistry},
  year={2012},
  volume={287},
  pages={28007 - 28016}
}
Background: HIGM-2 syndrome results from mutations spanning AID. Results: AID mutations are characterized biochemically and analyzed using a surrogate Apo3G structure. Conclusion: Catalytically active mutants retain salient enzymatic properties of WT AID; catalytically inactive mutants retain salient ssDNA binding properties of WT AID. Significance: We identify four structural classes of mutants and discuss the catalytic consequences of each mutation. Hyper-IgM syndrome type 2 stems from… Expand
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TLDR
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TLDR
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