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Serine/threonine protein kinases (EC 2.7.11.1) phosphorylate the OH group of serine or threonine (which have similar side chains). Activity of these protein kinases can be regulated by specific events (e.g., DNA damage), as well as numerous chemical signals, including cAMP/cGMP, diacylglycerol, and Ca 2+ /calmodulin.
Various other kinases act on small molecules such as lipids, carbohydrates, amino acids, and nucleotides, either for signaling or to prime them for metabolic pathways. Specific kinases are often named after their substrates. Protein kinases often have multiple substrates, and proteins can serve as substrates for more than one specific kinase.
Structure of Aurora A kinase (PDB: 3E5A) with labeled elements of secondary structure. The catalytic subunits of protein kinases are highly conserved, and the structures of over 280 of the approximately 494 kinase domains from 481 human genes have been determined, [8] leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases. [9]
Tyrosine kinases belong to a larger class of enzymes known as protein kinases which also attach phosphates to other amino acids such as serine and threonine. Phosphorylation of proteins by kinases is an important mechanism for communicating signals within a cell (signal transduction) and regulating cellular activity, such as cell division.
The DNA structure at left (schematic shown) will self-assemble into the structure visualized by atomic force microscopy at right. DNA nanotechnology is the field that seeks to design nanoscale structures using the molecular recognition properties of DNA molecules.
ATM serine/threonine kinase or Ataxia-telangiectasia mutated, symbol ATM, is a serine/threonine protein kinase that is recruited and activated by DNA double-strand breaks (canonical pathway), oxidative stress, topoisomerase cleavage complexes, splicing intermediates, R-loops and in some cases by single-strand DNA breaks. [5]
The chromatin structure functions and facilitates the packaging, organization and distribution of eukaryotic DNA. However, it has a negative impact on several fundamental biological processes such as transcription, replication and DNA repair by restricting the accessibility of certain enzymes and proteins.
695 12229 Ensembl ENSG00000010671 ENSMUSG00000031264 UniProt Q06187 P35991 RefSeq (mRNA) NM_001287345 NM_000061 NM_001287344 NM_013482 RefSeq (protein) NP_000052 NP_001274273 NP_001274274 NP_038510 Location (UCSC) Chr X: 101.35 – 101.39 Mb Chr X: 133.44 – 133.48 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Bruton's tyrosine kinase (abbreviated Btk or BTK), also known as ...