Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.13 (protein kinase C)
 49,245 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Zinc finger domains (ZnFs) are common, relatively small protein motifs that fold around one or more zinc ions. In addition to their role as a DNA-binding module, ZnFs have recently been shown to mediate protein:protein and protein:lipid interactions. This small zinc-ligating domain, often found in clusters containing fingers with different binding specificities, can facilitate multiple, often independent intermolecular interactions between nucleic acids and proteins. Classical ZnFs, typified by TFIIIA, ligate zinc via pairs of cysteine and histidine residues but there are at least 14 different classes of Zn fingers, which differ in the nature and arrangement of their zinc-binding residues. Some GATA-type ZnFs can bind to both DNA and a variety of other proteins. Thus proteins with multiple GATA-type fingers can play a complex role in regulating transcription through the interplay of these different binding selectivities and affinities. Other ZnFs have more specific functions, such as DNA-binding ZnFs in the nuclear hormone receptor proteins and small-molecule-binding ZnFs in protein kinase C. Some classes of ZnFs appear to act exclusively in protein-only interactions. These include the RING family of ZnFs that are involved in ubiquitination processes and in the assembly of large protein complexes, LIM, TAZ, and PHD domains. We review the similarities and differences in structure and functions of different ZnF classes and highlight the versatility of this fold.
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PMID:Zinc fingers--folds for many occasions. 1266 46

Interferon regulatory factor-1 (IRF-1), a putative tumor suppressor protein, is a transcriptional mediator of interferon-responsive signaling pathways that are involved in antiviral defense, apoptosis, immune response, and cell growth regulation. To delineate the IRF-1 domain responsible for transactivation, we performed a detailed deletion analysis of IRF-1. We found that the amino acid segment 217-260 was necessary and sufficient for transactivation. The structure of this region was predicted to be loop-helix-loop-sheet using the program PHD. Further studies indicated that casein kinase II and protein kinase C sites on each of the two loops are not important for transactivation, and a region containing amino acids 233-255 comprises the core activation domain. To verify the physiological role of segment 233-255, we constructed an IRF-1 deletion mutant lacking these amino acids and examined it using IRF-1 transactivation assay, fluorescence-activated cell sorting, and in situ beta-galactosidase staining techniques. From the results of these studies, we conclude that the amino acid segment 233-255 of IRF-1 comprises the core activation domain required for the physiological functions of IRF-1.
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PMID:Functional dissection of the transactivation domain of interferon regulatory factor-1. 1271 7