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Switching immune signals on and off.

Chu N, Cole PA - Elife (2015)

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, United States.

ABSTRACT

Bruton's tyrosine kinase, an enzyme that is important for B cell function, can be activated in a number of ways.

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Proposed model for the activation of Bruton's tyrosine kinase (Btk) by inositol hexaphosphate (IP6).Btk consists of four domains: PH-TH (green), SH3 (blue), SH2 (purple) and the kinase domain (orange), and Wang et al. have studied how the interactions between these domains regulate the activity of the enzyme. For example, the binding of IP6 to an allosteric surface of the PH-TH domain (which contains the K36, K49 and R52 residues) can stimulate a pair of Btk molecules to form a dimer. This results in the two kinase domains phosphorylating each other at the Tyr 551 residue (Y551), which activates Btk.
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fig1: Proposed model for the activation of Bruton's tyrosine kinase (Btk) by inositol hexaphosphate (IP6).Btk consists of four domains: PH-TH (green), SH3 (blue), SH2 (purple) and the kinase domain (orange), and Wang et al. have studied how the interactions between these domains regulate the activity of the enzyme. For example, the binding of IP6 to an allosteric surface of the PH-TH domain (which contains the K36, K49 and R52 residues) can stimulate a pair of Btk molecules to form a dimer. This results in the two kinase domains phosphorylating each other at the Tyr 551 residue (Y551), which activates Btk.

Mentions: Btk is composed of a series of different domains. The kinase domain, which catalyzes the phosphorylation of proteins, is connected via domains called SH2 and SH3 to the PH-TH domain (Figure 1). While the three-dimensional structures of the isolated Btk domains have previously been determined, it has not been clear how these domains interact with each other and how they regulate the kinase domain. It has been proposed that Btk is recruited to cellular membranes by a molecule embedded in the membrane called phosphatidyl inositol triphosphate (PIP3). This phospholipid engages with the PH-TH domain, and somehow activates the Btk kinase domain so that it phosphorylates itself and/or causes it to be activated by other tyrosine kinases (Mohamed et al., 2009).Figure 1.Proposed model for the activation of Bruton's tyrosine kinase (Btk) by inositol hexaphosphate (IP6).


Switching immune signals on and off.

Chu N, Cole PA - Elife (2015)

Proposed model for the activation of Bruton's tyrosine kinase (Btk) by inositol hexaphosphate (IP6).Btk consists of four domains: PH-TH (green), SH3 (blue), SH2 (purple) and the kinase domain (orange), and Wang et al. have studied how the interactions between these domains regulate the activity of the enzyme. For example, the binding of IP6 to an allosteric surface of the PH-TH domain (which contains the K36, K49 and R52 residues) can stimulate a pair of Btk molecules to form a dimer. This results in the two kinase domains phosphorylating each other at the Tyr 551 residue (Y551), which activates Btk.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4384531&req=5

fig1: Proposed model for the activation of Bruton's tyrosine kinase (Btk) by inositol hexaphosphate (IP6).Btk consists of four domains: PH-TH (green), SH3 (blue), SH2 (purple) and the kinase domain (orange), and Wang et al. have studied how the interactions between these domains regulate the activity of the enzyme. For example, the binding of IP6 to an allosteric surface of the PH-TH domain (which contains the K36, K49 and R52 residues) can stimulate a pair of Btk molecules to form a dimer. This results in the two kinase domains phosphorylating each other at the Tyr 551 residue (Y551), which activates Btk.
Mentions: Btk is composed of a series of different domains. The kinase domain, which catalyzes the phosphorylation of proteins, is connected via domains called SH2 and SH3 to the PH-TH domain (Figure 1). While the three-dimensional structures of the isolated Btk domains have previously been determined, it has not been clear how these domains interact with each other and how they regulate the kinase domain. It has been proposed that Btk is recruited to cellular membranes by a molecule embedded in the membrane called phosphatidyl inositol triphosphate (PIP3). This phospholipid engages with the PH-TH domain, and somehow activates the Btk kinase domain so that it phosphorylates itself and/or causes it to be activated by other tyrosine kinases (Mohamed et al., 2009).Figure 1.Proposed model for the activation of Bruton's tyrosine kinase (Btk) by inositol hexaphosphate (IP6).

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, United States.

ABSTRACT

Bruton's tyrosine kinase, an enzyme that is important for B cell function, can be activated in a number of ways.

Show MeSH