![]() These results are in agreement with recent reports on the protein structure of the AID homolog APOBEC3G, suggesting a similar protein composition. Indeed, by generating homologous amino acid replacements, CSR activity could be restored. Interestingly, the most debilitating mutations concentrated on hydrophobic amino acids, suggesting a structural role for this part of the protein. A defect in deaminase activity was found to underlie this CSR deficiency. The results from this analysis pointed to several amino acids that are required for class switch recombination (CSR), without perturbing cellular localization or nucleocytoplasmic shuttling. With the generation of single point mutations, we studied the structure-function relationship of the amino acids that are commonly absent from all described splice variants. Recently, conflicting results were reported on the hypermutation activity of activation-induced cytidine deaminase (AID) splice variants. ![]()
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