Open AccessZinc fingers: DNA binding and protein-protein interactions
Author(s) -
Óscar León,
Monica J. Roth
Publication year - 2000
Publication title -
biological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.127
H-Index - 55
eISSN - 0717-6287
pISSN - 0716-9760
DOI - 10.4067/s0716-97602000000100009
Subject(s) - zinc finger , zinc , lim domain , nucleic acid , protein structure , biochemistry , dna , protein domain , chemistry , protein structure prediction , biology , biophysics , gene , transcription factor , organic chemistry
The zinc finger domain is a very ubiquitous structural element whose hallmark is the coordination of a zinc atom by several amino acid residues (cysteines and histidines, and occasionally aspartate and glutamate). These structural elements are associated with protein-nucleic acid recognition as well as protein-protein interactions. The purpose of this review is to examine recent data on the DNA and protein binding properties of a few zinc fingers whose three dimensional structure is known.