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  2. Protein kinase - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase

    Above is a ball-and-stick model of the inorganic phosphate molecule (H PO 4 2−).Colour coding: P (orange); O (red); H (white). The chemical activity of a protein kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group.

  3. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    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.

  4. Tyrosine kinase - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_kinase

    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.

  5. Protein kinase domain - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase_domain

    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 500 human kinase domains have been determined, [8] leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases. [9]

  6. Receptor tyrosine kinase - Wikipedia

    en.wikipedia.org/wiki/Receptor_tyrosine_kinase

    Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome , 58 encode receptor tyrosine kinase proteins. [ 1 ]

  7. Src family kinase - Wikipedia

    en.wikipedia.org/wiki/Src_family_kinase

    Src family kinases contain six distinct domains including a myristoylated N-terminal segment, an SH2 domain, an SH3 domain, a linker region, a tyrosine kinase domain, and a C-terminal tail. Src kinases are known for having a characteristically short C-terminal tail that contains an autoinhibitory phosphorylation site.

  8. Protein kinase C - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase_C

    For example, the two atypical PKC isoforms, ζ and ι/λ, are 84% identical (Selbie et al., 1993). Of the over-30 protein kinase structures whose crystal structure has been revealed, all have the same basic organization. They are a bilobal structure with a β sheet comprising the N-terminal lobe and an α helix constituting the C-terminal lobe.

  9. Two-component regulatory system - Wikipedia

    en.wikipedia.org/wiki/Two-component_regulatory...

    Two-component systems accomplish signal transduction through the phosphorylation of a response regulator (RR) by a histidine kinase (HK). Histidine kinases are typically homodimeric transmembrane proteins containing a histidine phosphotransfer domain and an ATP binding domain, though there are reported examples of histidine kinases in the atypical HWE and HisKA2 families that are not ...