Zinc finger proteins: new insights into structural and functional diversity.
Zinc finger proteins are among the most abundant proteins in eukaryotic genomes. Their functions are extraordinarily diverse and include DNA recognition, RNA packaging, transcriptional activation, regulation of apoptosis, protein folding and assembly, and lipid binding. Zinc finger structures are as diverse as their functions. Structures have recently been reported for many new zinc finger domains with novel topologies, providing important insights into structure/function relationships. In addition, new structural studies of proteins containing the classical Cys(2)His(2) zinc finger motif have led to novel insights into mechanisms of DNA binding and to a better understanding of their broader functions in transcriptional regulation.
Laity
J H
JH
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Lee
B M
BM
Wright
P E
PE
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D012321:DNA-Directed RNA Polymerases; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D051034:Inhibitor of Apoptosis Proteins; D020449:Repetitive Sequences, Amino Acid; D012269:Ribosomal Proteins; D015398:Signal Transduction; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D014764:Viral Proteins; D015032:Zinc; D016335:Zinc Fingers / Q000502:physiology*
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D051034:Inhibitor of Apoptosis Proteins; D012269:Ribosomal Proteins; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D014764:Viral Proteins; C086430:inhibitor of apoptosis, Nucleopolyhedrovirus; D012321:DNA-Directed RNA Polymerases; D015032:Zinc