APOBEC
From Wikipedia, the free encyclopedia
Example of a member of the APOBEC family, APOBEC-2. A cytidine deaminase from
Homo Sapiens.
[1]
APOBEC ("apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like") is a family of evolutionary conserved proteins:
A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalyitc domain. More specifically, the catalytic domain is a zinc dependent cytidine deaminase domain and is essential for cytidine deamination. RNA editing by APOBEC-1 requires homodimerisation and this complex interacts with RNA binding proteins to from the editosome.[2]
[edit] Family members
Human genes encoding members of the APOBEC protein family include:
[edit] References
- ^ PDB 2NYT; Prochnow, C., Bransteitter, R., Klein, M.G., Goodman, M.F., Chen, X.S. (2007). "The APOBEC-2 crystal structure and functional implications for the deaminase AID.". Nature 445 (7126): 447–451. doi:10.1038/nature05492. PMID 17187054. ; rendered using PyMOL.
- ^ Wedekind JE, Dance GS, Sowden MP, Smith HC (April 2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business". Trends Genet. 19 (4): 207–16. doi:10.1016/S0168-9525(03)00054-4. PMID 12683974.
This article incorporates text from the public domain Pfam and InterPro IPR013158
