What has an SH2 domain?
Src homology 2 (SH2) domains are protein modules (of approximately 100 amino acids) found in many proteins involved in tyrosine kinase signalling cascades. Their function is to bind tyrosine-phosphorylated sequences in specific protein targets.
Does Akt have SH2 domain?
Grb10 and Akt interact constitutively via their PH domains (Jahn et al., 2002). Via its SH2 domain, Grb10 also binds phos- phorylated tyrosine residues in several ligand-activated tyrosine kinase receptors, including the insulin receptor (IR), the insulin-like growth factor-I receptor (IGF-IR) and c-kit.
What signal transduction functions do SH2 domains in proteins serve?
SH2 domains allow proteins containing those domains to dock to phosphorylated tyrosine residues on other proteins. SH2 domains are commonly found in adaptor proteins that aid in the signal transduction of receptor tyrosine kinase pathways.
Is the SH2 domain hydrophobic?
The results suggest that the SH2-domain-mediated activation of Csk is dependent on the binding of the beta3-alphaC loop Ala228 to the hydrophobic pocket formed by the side chains of Tyr116, Tyr133, Leu138, and Leu149 on the surface of the SH2 domain. Copyright (c) 2010 Elsevier Ltd.
What type of protein is RAS?
Ras, from “Rat sarcoma virus”, is a family of related proteins that are expressed in all animal cell lineages and organs. All Ras protein family members belong to a class of protein called small GTPase, and are involved in transmitting signals within cells (cellular signal transduction).
Are PKB and Akt the same?
Protein kinase B (PKB), also known as Akt, is the collective name of a set of three serine/threonine-specific protein kinases that play key roles in multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration.
Is Akt an oncogene?
AKT was first discovered in the 1970s as an oncogene transduced by the transforming retrovirus (AKT‐8), which was isolated from an AKR mouse thymoma cell line and first molecularly cloned in 1991.
What adaptor protein binds the phosphorylated receptor using its SH2 domain?
Gads
Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc. Oncogene. 1998 Dec 17;17(24):3073-82. doi: 10.1038/sj.
Is Ras a heterotrimeric G protein?
Heterotrimeric G proteins (αβγ) and Ras proteins are activated by cell-surface receptors that sense extracellular signals. Both sets of proteins were traditionally thought to be constrained to the plasma membrane and some intracellular membranes.
What are the functions of the SH2 domain?
Other SH2 domain proteins are devoid of intrinsic enzymatic activity and serve as adaptors that connect the activated receptors with downstream signaling molecules. Adaptors often have additional domains that mediate interactions with other molecules, such as the SH3 and PH domains [32].
Are there any phosphatases that contain SH2 domains?
The SH2 domain-containing phosphatases (Shps) belong to a class of non-transmembrane protein tyrosine phosphatases that contain two N-terminal SH2 domains.119 There are two vertebrate Shps: SHP1 and SHP2.
Where are the SH2 domains located in PDBsum?
PDBsum. structure summary. The SH2 ( S rc H omology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. SH2 domains allow proteins containing those domains to dock to phosphorylated tyrosine residues on other proteins.
How are SH2 domains related to phospho Tyr binding?
S rc- h omology 2 ( SH2) domains are modules of approximately 100 amino acids that bind to specific phospho (pY)-containing peptide motifs. Conventional SH2 domains have a conserved pocket that recognizes pY, and a more variable pocket that binds 3-6 residues C-terminal to the pY to confer specificity.