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Histidine-specific protein kinases are structurally distinct from other protein kinases and are found in prokaryotes, fungi, and plants as part of a two-component signal transduction mechanism: a phosphate group from ATP is first added to a histidine residue within the kinase, then transferred to an aspartate residue on a receiver domain on a ...
Src-associated adaptor protein Skap2 with 1u5e code. Signal transducing adaptor proteins (STAPs) are proteins that are accessory to main proteins in a signal transduction pathway. [1] Adaptor proteins contain a variety of protein-binding modules that link protein-binding partners together and facilitate the creation of larger signaling complexes.
KH domain-containing, RNA-binding, signal transduction-associated protein 1 is a protein that in humans is encoded by the KHDRBS1 gene. [5] [6]This gene encodes a member of the K homology domain-containing, RNA-binding, signal transduction-associated protein family.
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 ...
The SH2 (Src Homology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein [2] and in many other intracellular signal-transducing proteins. [3] SH2 domains bind to phosphorylated tyrosine residues on other proteins, modifying the function or activity of the SH2-containing protein. The SH2 domain may be ...
G protein-coupled receptors are involved in many diseases, and thus are the targets of many modern medicinal drugs. [16] There are two principal signal transduction pathways involving the G-protein coupled receptors: the cAMP signaling pathway and the phosphatidylinositol signaling pathway. [17] Both are mediated via G protein activation. The G ...
This signal is transmitted via a direct interaction between Fz and Dsh. Dsh proteins are present in all organisms and they all share the following highly conserved protein domains: an amino-terminal DIX domain, a central PDZ domain, and a carboxy-terminal DEP domain. These different domains are important because after Dsh, the Wnt signal can ...
In 1995 proteins were found containing a second type of P.Tyr-binding domain, PTB, in RTK signaling. Gradually the number of identified tyrosine kinases and receptor tyrosine kinases grew. As of 2002, of the 90 known human tyrosine kinases, 58 were RTKs, and opposing the action of the tyrosine kinases were 108 protein phosphatases that can ...