APOBEC
| APOBEC-like N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | APOBEC_N | ||||||||
| Pfam | PF08210 | ||||||||
| InterPro | IPR013158 | ||||||||
| |||||||||
| APOBEC-like C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | APOBEC_C | ||||||||
| Pfam | PF05240 | ||||||||
| InterPro | IPR007904 | ||||||||
| |||||||||
APOBEC ("apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like") is a family of evolutionarily conserved cytidine deaminases.
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 pseudocatalytic 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 form the editosome.[2]
In humans/mammals they help protect from viral infections.[3] These enzymes, when misregulated, are a major source of mutation in numerous cancer types.[3]
A 2013 review discussed the structural and biophysical aspects of APOBEC3 family enzymes.[4] Much of the APOBEC protein features are described in the widely studied APOBEC3G's page.
Family members
Human genes encoding members of the APOBEC protein family include:
- APOBEC1
- APOBEC2
- APOBEC3A
- APOBEC3B
- APOBEC3C
- APOBEC3D ("APOBEC3E" now refers to this)
- APOBEC3F
- APOBEC3G
- APOBEC3H
- APOBEC4
- Activation-induced (cytidine) deaminase
References
- ↑ PDB: 2NYT; Prochnow, C.; Bransteitter, R.; Klein, M.G.; Goodman, M.F.; Chen, X.S.; functional implications for the deaminase AID. (2007). "The APOBEC-2 crystal structure". Nature. 445 (7126): 447–451. PMID 17187054. doi:10.1038/nature05492.; 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. PMID 12683974. doi:10.1016/S0168-9525(03)00054-4.
- 1 2 Unexpected DNA-Binding Mechanism Suggests Ways to Block Enzyme Activity in Cancer
- ↑ Jaguva Vasudevan, AA; Smits SH; Höppner A; Häussinger D; Koenig BW; Münk C. (June 2013). "Structural features of antiviral DNA cytidine deaminases". Biol Chem. 394 (11): 1357–1370. PMID 23787464. doi:10.1515/hsz-2013-0165.
This article incorporates text from the public domain Pfam and InterPro IPR013158