EC Number   |
|---|
   3.5.4.38 | generation of a panel of free or DNA-bound AID models based on eight recently resolved APOBEC isoform structures. The majority of AID:DNA complexes would be inactive due to substrate binding such that a cytidine is not positioned for deamination. Most AID conformations exhibit fully or partially occluded catalytic pockets |
| 3.5.4.38 | generation of a panel of free or DNA-bound AID models based on eight resolved APOBEC structures. The majority of AID:DNA complexes would be inactive due to substrate binding such that a cytidine is not positioned for deamination. Most AID conformations exhibit fully or partially occluded catalytic pockets |
| 3.5.4.38 | hanging drop vapor diffusion method |
| 3.5.4.38 | hanging drop vapor diffusion method, APOBEC3B catalytic domain crystal structures including a dCMP-bound form |
| 3.5.4.38 | modeling of structure. Residue Arg211 in loop 1 is the gatekeeper coordinating DNA. ssDNA binds to the C-terminal domain in a U-shape, and loop 1 undergoes major conformational changes to open up the active site for DNA binding. Residue D314 defines substrate specificity for thymidine over cytidine at -1 position. An auto-inhibited conformation in the C-terminal domain restricts access and binding of DNA to the active site |
| 3.5.4.38 | sitting drop vapor diffusion method at 4°C, crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA at 1.86 A resolution |
| 3.5.4.38 | sitting drop vapor diffusion technique at 4°C, crystal structure of enzyme variant AIDv(DELTA15), at 2.8 A resolution |
| 3.5.4.38 | sitting drop vapor-diffusion method, crystal structure of the C-terminal catalytic domain of the enzyme (APOBEC3F) in complex with a 10 nucleotide ssDNA composed of a poly-thymine sequence |
