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Kinase tyrosine

Tyrosine kinase receptors are important enzyme-linked receptors... [Pg.270]

There are five known classes of enzyme-linked receptors (1) receptor tyrosine kinases, which phosphorylate specific tyrosine residues on intracellular signaling proteins (2) tyrosine kinase-associated receptors, such as the prolactin and growth hormone receptors we have already discussed, which... [Pg.270]

Figure 13.24 Six subfamilies of receptor tyrosine kinases involved in cell growth and differentiation. Only one or two members of each subfamily are indicated. Note that the tyrosine kinase domain is interrupted by a "kinase insert region" in some of the subfamilies. The functional significance of the cysteine-rich and immunoglobulin-like domains is unknown. Figure 13.24 Six subfamilies of receptor tyrosine kinases involved in cell growth and differentiation. Only one or two members of each subfamily are indicated. Note that the tyrosine kinase domain is interrupted by a "kinase insert region" in some of the subfamilies. The functional significance of the cysteine-rich and immunoglobulin-like domains is unknown.
Figure 13.26 Schematic diagram of the SH2 domain from the Src tyrosine kinase with bound peptide. The SH2 domain (blue) comprises a central p sheet surrounded by two a helices. Three positively charged residues (green) are involved in binding the phosphotyrosine moiety of the bound peptide (red). (Adapted from G. Waksman et al.. Cell 72 779-790, 1993.)... Figure 13.26 Schematic diagram of the SH2 domain from the Src tyrosine kinase with bound peptide. The SH2 domain (blue) comprises a central p sheet surrounded by two a helices. Three positively charged residues (green) are involved in binding the phosphotyrosine moiety of the bound peptide (red). (Adapted from G. Waksman et al.. Cell 72 779-790, 1993.)...
Src tyrosine kinases comprise SH2 and SH3 domains in addition to a tyrosine kinase... [Pg.275]

The polypeptide chain of Src tyrosine kinase, and related family members, comprises an N-terminal "unique" region, which directs membrane association and other as yet unknown functions, followed by a SH3 domain, a SH2 domain, and the two lobes of the protein kinase. Members of this family can be phosphorylated at two important tyrosine residues—one in the "activation loop" of the kinase domain (Tyr 419 in c-Src), the other in a short... [Pg.275]

Figure 13.30 Ribbon diagram of the structure of Src tyrosine kinase. The structure is divided in three units starting from the N-terminus an SH3 domain (green), an SH2 domain (blue), and a tyrosine kinase (orange) that is divided into two domains and has the same fold as the cyclin dependent kinase described in Chapter 6 (see Figure 6.16a). The linker region (red) between SH2 and the kinase is bound to SH3 in a polyproline helical conformation. A tyrosine residue in the carboxy tail of the kinase is phosphorylated and bound to SH2 in its phosphotyrosine-binding site. A disordered part of the activation segment in the kinase is dashed. (Adapted from W. Xu et al.. Nature 385 595-602, 1997.)... Figure 13.30 Ribbon diagram of the structure of Src tyrosine kinase. The structure is divided in three units starting from the N-terminus an SH3 domain (green), an SH2 domain (blue), and a tyrosine kinase (orange) that is divided into two domains and has the same fold as the cyclin dependent kinase described in Chapter 6 (see Figure 6.16a). The linker region (red) between SH2 and the kinase is bound to SH3 in a polyproline helical conformation. A tyrosine residue in the carboxy tail of the kinase is phosphorylated and bound to SH2 in its phosphotyrosine-binding site. A disordered part of the activation segment in the kinase is dashed. (Adapted from W. Xu et al.. Nature 385 595-602, 1997.)...
Figure 13.31 Space-filling diagram of Src tyrosine kinase in the same view as Figure 13.30. The SH2 domain makes only a few contacts with the rest of the molecule except for the tail region of the kinase. The SH3 domain contacts the N-domain of the kinase in addition to the linker region. There are extensive contacts between the N- and C-domains of the kinase. (Adapted from W. Xu et al., Nature 385 596-602, 1997.)... Figure 13.31 Space-filling diagram of Src tyrosine kinase in the same view as Figure 13.30. The SH2 domain makes only a few contacts with the rest of the molecule except for the tail region of the kinase. The SH3 domain contacts the N-domain of the kinase in addition to the linker region. There are extensive contacts between the N- and C-domains of the kinase. (Adapted from W. Xu et al., Nature 385 596-602, 1997.)...
C-terminal lobes of the tyrosine kinase are similar to those of cyclin-depen-dent kinase described in Chapter 6 (see Figure 6.16a), while the SH2 and SH3 domains of Src and Hck have structures very similar to those of the isolated domains (see Figures 13.26 and 13.28a). [Pg.277]

Figure 13.32 Regulation of the catalytic activity of members of the Src family of tyrosine kinases, (a) The inactive form based on structure determinations. Helix aC is in a position and orientation where the catalytically important Glu residue is facing away from the active site. The activation segment has a conformation that through steric contacts blocks the catalytically competent positioning of helix aC. (b) A hypothetical active conformation based on comparisons with the active forms of other similar protein kinases. The linker region is released from SH3, and the activation segment changes its structure to allow helix aC to move and bring the Glu residue into the active site in contact with an important Lys residue. Figure 13.32 Regulation of the catalytic activity of members of the Src family of tyrosine kinases, (a) The inactive form based on structure determinations. Helix aC is in a position and orientation where the catalytically important Glu residue is facing away from the active site. The activation segment has a conformation that through steric contacts blocks the catalytically competent positioning of helix aC. (b) A hypothetical active conformation based on comparisons with the active forms of other similar protein kinases. The linker region is released from SH3, and the activation segment changes its structure to allow helix aC to move and bring the Glu residue into the active site in contact with an important Lys residue.
Src tyrosine kinase contains both an SH2 and an SH3 domain linked to a tyrosine kinase unit with a structure similar to other protein kinases. The phosphorylated form of the kinase is inactivated by binding of a phosphoty-rosine in the C-terminal tail to its own SH2 domain. In addition the linker region between the SH2 domain and the kinase is bound in a polyproline II conformation to the SH3 domain. These interactions lock regions of the active site into a nonproductive conformation. Dephosphorylation or mutation of the C-terminal tyrosine abolishes this autoinactivation. [Pg.280]

Sicheri, R, Moarefi, 1., Kuriyan, J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385 602-609, 1997. [Pg.281]


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ABL tyrosine kinase

Abelson tyrosine kinase

Activation of Cytoplasmic Tyrosine Kinases

Adhesion tyrosine kinase

Allosteric enzymes receptor tyrosine kinase

Anticancer drugs protein tyrosine kinases

Associated tyrosine kinase

Autophosphorylation protein tyrosine kinases

BTK, Bruton’s Tyrosine Kinase

Bcr-Abl-tyrosine kinase inhibitor

Bcr-abl tyrosine kinase

Bisubstrate tyrosine kinase inhibitors

Breast Cancer Human Epidermal Growth Factor Tyrosine Kinase Inhibitors

Bruton s tyrosine kinase

Bruton tyrosine kinase

C-Abl tyrosine kinase

C-Kit receptor tyrosine kinase

Cancer chemotherapy tyrosine kinase inhibitors

Cancer, treatment using tyrosine kinase inhibitors

Cancer, treatment using tyrosine kinase receptor inhibitors

Cell death tyrosine kinases activated apoptotic

Cellular signaling receptor tyrosine kinase

Chemotherapy tyrosine kinase inhibitors

Classes tyrosine kinase receptors

Cytoplasmic Tyrosine Kinases

Cytoplasmic tyrosine kinase-linked receptors

Cytosolic tyrosine-kinases

Dimerization protein tyrosine kinases

Dimerization receptor tyrosine kinases

EFGR tyrosine kinase

EFGR tyrosine kinase inhibitor

EGFR tyrosine kinase

EGFR tyrosine kinase inhibitor

Effector Proteins of the Receptor Tyrosine Kinases

Eph Receptor Tyrosine Kinase

EphB4 Tyrosine Kinase (Cancer)

Epidermal growth factor receptor tyrosine kinase

Fms-like tyrosine kinase

Fyn tyrosine kinase

Genistein, tyrosine kinase inhibition

Growth factors protein tyrosine kinase domain

Halistanol sulfate pp60v-src protein tyrosine kinase

Hormone-activated receptor tyrosine kinase

Imaging tyrosine kinase receptor

Imidazoles tyrosine kinase inhibitor

Inhibitors, spleen tyrosine kinase

Insulin receptor /3-subunit tyrosine kinase

Insulin receptor protein tyrosine kinase domain structure

Insulin receptor signal transduction tyrosine kinase

Insulin receptor tyrosine kinase

Insulin receptor tyrosine kinase domain

Insulin receptor tyrosine specific protein kinase

Jak2, tyrosine kinase

Janus tyrosine kinase

Kinases serine/threonine/ tyrosine

Lck tyrosine kinase

Ligand-binding domains receptor tyrosine kinases

MET receptor tyrosine kinase

Membrane receptors with associated tyrosine kinase

Multiple tyrosine kinase inhibitor

Natural tyrosine kinase inhibitor

Neurotrophic tyrosine receptor kinase

Non-receptor tyrosine kinases

Nonreceptor Tyrosine-specific Protein Kinases

Nonreceptor protein tyrosine kinases , signaling

Nonreceptor tyrosine kinase

Nonreceptor tyrosine kinase Activation

Nonreceptor tyrosine kinase Function

Nonreceptor tyrosine kinase Structure

Of tyrosine kinase inhibitor

Phosphorylation tyrosine kinase activity

Platelet activation tyrosine kinase

Platelet-derived growth factor receptor tyrosine kinase inhibition

Platelets activation: tyrosine kinase phosphorylation

Pp60v-src protein tyrosine kinase

Proline-rich tyrosine kinase

Protein tyrosine kinase (PTK)

Protein tyrosine kinases

Protein tyrosine kinases binding domains

Protein tyrosine kinases characteristics

Protein tyrosine kinases classes

Protein tyrosine kinases classification

Protein tyrosine kinases cross-linking

Protein tyrosine kinases cytoplasmic domain

Protein tyrosine kinases description

Protein tyrosine kinases extracellular region

Protein tyrosine kinases family

Protein tyrosine kinases inactivation

Protein tyrosine kinases intracellular calcium concentration

Protein tyrosine kinases intracellular second messengers

Protein tyrosine kinases mitogen-activated

Protein tyrosine kinases nonreceptor

Protein tyrosine kinases oncogene studies

Protein tyrosine kinases pharmacological regulation

Protein tyrosine kinases phosphorylation

Protein tyrosine kinases receptor

Protein tyrosine kinases receptors that contain

Protein tyrosine kinases regulation

Protein tyrosine kinases regulatory domain

Protein tyrosine kinases schematic diagram

Protein tyrosine kinases signaling complexes

Protein tyrosine kinases translocation

Protein tyrosine kinases transmembrane domain

Protein tyrosine kinases vascular endothelial growth factor

Protein tyrosine kinases, activation

Protein-tyrosine Kinase Inhibitors

Protein-tyrosine kinase activity

Protein-tyrosine kinase activity of Koelreuteria henryi

Protein-tyrosine kinase activity of flavonoid aglycones

Protein-tyrosine kinase activity of glycosides

Protein-tyrosine kinase inhibitory

Protein-tyrosine kinase inhibitory activities

Protein-tyrosine kinases inhibition by piceatannol

Reactive oxygen species receptor tyrosine kinases

Receptor Activation, Tyrosine Kinase Activity, and in Cultured Vascular Smooth Muscle Cells

Receptor protein tyrosine kinases, signal pathways

Receptor tyrosine kinase Activation

Receptor tyrosine kinase Effector proteins

Receptor tyrosine kinase Function

Receptor tyrosine kinase Heterodimer

Receptor tyrosine kinase Oligomerization

Receptor tyrosine kinase Structure

Receptor tyrosine kinase activity, insulin

Receptor tyrosine kinase antagonists

Receptor tyrosine kinase domain structure

Receptor tyrosine kinase family

Receptor tyrosine kinase inhibitor

Receptor tyrosine kinases

Receptor tyrosine kinases , signaling

Receptor tyrosine kinases biological roles

Receptor tyrosine kinases ligand-induced dimerization

Receptor tyrosine kinases malignancy

Receptor tyrosine kinases mechanisms

Receptor tyrosine kinases phosphorylation, regulation

Receptor tyrosine kinases progression

Receptor tyrosine kinases recognition

Receptor tyrosine kinases signal transduction

Receptor tyrosine kinases signaling pathways

Receptor tyrosine kinases signaling trigger

Receptors cytosolic tyrosine-kinases

Receptors tyrosine kinase, coupling

Receptors tyrosine kinase-containing

Receptors tyrosine-specific kinase

Receptors with Associated Tyrosine Kinase Activity

Receptors with tyrosine kinase activity

Role of Tyrosine Kinase

Second messengers receptor tyrosine kinases

Signal Pathways Operated by Receptor Protein Tyrosine Kinase

Signal Transmission via Transmembrane Receptors with Tyrosine-specific Protein Kinase Activity

Signal transduction tyrosine kinases

Signaling pathways protein tyrosine kinases

Signaling pathways tyrosine kinases

Spleen tyrosine kinase

Src family protein tyrosine kinases

Src family, of protein tyrosine kinases

Src tyrosine kinase

Structure and Activation of the Tyrosine Kinase Domain

Structure and General Function of Nonreceptor Tyrosine Kinases

Subject tyrosine kinase

The Janus Family Tyrosine Kinases-Signal Transducers and Activators of Transcription Signaling Pathway

Tie2 tyrosine kinase inhibitor

Transmembrane receptor Associated tyrosine kinase

Transmembrane receptor Intrinsic tyrosine kinase

Transmembrane tyrosine kinase receptor

Tumor antigen Tyrosine kinase

Tyrosine -specific protein kinase

Tyrosine kinase activity

Tyrosine kinase antagonists

Tyrosine kinase anti-VEGF therapy

Tyrosine kinase biochemical action

Tyrosine kinase classification

Tyrosine kinase domain

Tyrosine kinase inhibition

Tyrosine kinase inhibitor therapy

Tyrosine kinase inhibitors

Tyrosine kinase inhibitors Philadelphia chromosome

Tyrosine kinase inhibitors biological activity

Tyrosine kinase inhibitors imatinib mesylate

Tyrosine kinase inhibitors in cancer therapy

Tyrosine kinase inhibitors molecular modeling

Tyrosine kinase plant-derived inhibitors

Tyrosine kinase receptors, drug

Tyrosine kinase receptors, drug development

Tyrosine kinase, phosphorylation site

Tyrosine kinase-associated receptors

Tyrosine kinase-containing

Tyrosine kinase-like group of kinases

Tyrosine kinase-linked receptors

Tyrosine kinase-mediated signalling

Tyrosine kinases inflammatory diseases

Tyrosine kinases malignancy

Tyrosine kinases phosphorylation

Tyrosine kinases plate

Tyrosine protein kinase , and

Tyrosine-specific kinase inhibitor

Tyrosine-specific kinases

Tyrosines tyrosine kinase

Tyrosines tyrosine kinase

VEGF receptor tyrosine kinase inhibitors

Vascular endothelial growth factor tyrosine kinase inhibitors

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