Cys2His2 zinc finger protein family: classification, functions, and major members.
Biochemistry (Mosc)
; 77(3): 217-26, 2012 Mar.
Article
en En
| MEDLINE
| ID: mdl-22803940
ABSTRACT
Cys2His2 (C2H2)-type zinc fingers are widespread DNA binding motifs in eukaryotic transcription factors. Zinc fingers are short protein motifs composed of two or three ß-layers and one α-helix. Two cysteine and two histidine residues located in certain positions bind zinc to stabilize the structure. Four other amino acid residues localized in specific positions in the N-terminal region of the α-helix participate in DNA binding by interacting with hydrogen donors and acceptors exposed in the DNA major groove. The number of zinc fingers in a single protein can vary over a wide range, thus enabling variability of target DNA sequences. Besides DNA binding, zinc fingers can also provide protein-protein and RNA-protein interactions. For the most part, proteins containing the C2H2-type zinc fingers are trans regulators of gene expression that play an important role in cellular processes such as development, differentiation, and suppression of malignant cell transformation (oncosuppression).
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Factores de Transcripción
/
Familia de Multigenes
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochemistry (Mosc)
Año:
2012
Tipo del documento:
Article
País de afiliación:
Rusia