Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Cyclins

In free CDK2 the active site cleft is blocked by the T-loop and Thr 160 is buried (Figure 6.20a). Substrates cannot bind and Thr 160 cannot be phosphorylated consequently free CDK2 is inactive. The conformational changes induced by cyclin A binding not only expose the active site cleft so that ATP and protein substrates can bind but also rearrange essential active site residues to make the enzyme catalytically competent (Figure 6.20b). In addition Thr... [Pg.108]

Figure 6.18 The PSTAIRE helix undergoes a major conformational change when CDK2 binds to cyclin A. In the inactive free CDK2 (yellow) the active site residue Glu 51 is far from the active site. Upon binding of cyclin A to CDK2 the PSTAIRE helix (hiue) rotates 90° and changes its position so that Glu 51 becomes positioned into the active site. (Adapted from P.D. Jeffry et al.. Nature 376 313-320, 1995.)... Figure 6.18 The PSTAIRE helix undergoes a major conformational change when CDK2 binds to cyclin A. In the inactive free CDK2 (yellow) the active site residue Glu 51 is far from the active site. Upon binding of cyclin A to CDK2 the PSTAIRE helix (hiue) rotates 90° and changes its position so that Glu 51 becomes positioned into the active site. (Adapted from P.D. Jeffry et al.. Nature 376 313-320, 1995.)...
Figure 6.20 Space-filling diagram illustrating the structural changes of CDK2 upon cyclin binding, (a) The active site is in a cleft between the N-terminal domain (blue) and the C-terminal domain (purple). In the inactive form this site is blocked by the T-loop. Figure 6.20 Space-filling diagram illustrating the structural changes of CDK2 upon cyclin binding, (a) The active site is in a cleft between the N-terminal domain (blue) and the C-terminal domain (purple). In the inactive form this site is blocked by the T-loop.
Radzio-Andzelm, E.R., Few, J., Taylor, S. Bound to activate conformational consequences of cyclin binding to CDK2. Structure 3 1135-1141, 1995. [Pg.119]

De Bondt, H.E., et al. Crystal structure of cyclin-depen-dent kinase 2. Nature 363 595-602, 1993. [Pg.119]

TFIIB is arranged in two domains, both of which have the cyclin fold described in Chapter 6. Both domains bind to the TBP-TATA box complex at the C-terminal stirrup and helix of TBP. The phosphate and sugar moities of DNA form extensive non-sequence-specific contacts with TFIIB both upstream and downstream of the middle of the TATA box. [Pg.159]

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.)...
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]

A number of kinase structures have been determined in various catalytic states. For example, structures of the cyclin-dependent kinase, CDK2, in its inactive state and in a partially active state after cyclin binding have been discussed in Chapter 6. The most thoroughly studied kinase is the cyclic AMP-dependent protein kinase the structure of both the inactive and the active... [Pg.277]

Reductive Methyiation of 7-IN,N -Dicarbobenzyloxyhydrazino)-6-Demethyl-6-Deoxytetra-cycline to 7-Dimetbylamino-6-Demetbyl-6-Deoxytetracycline A solution of 100 mg of 7-(N,N -dicarbobenzyloxyhydrazino)-6-demethyl-6-deoxytetracycline in 2.6 ml of methanol,... [Pg.1030]

Cell Cycle Control. Figure 1 Cell cycle regulation by Cyclin dependent kinases (CDKs). Different cyclins bound to different CDKs promote the transition from one cell cycle phase into another. CDK-dependent phosphorylation of Rb is required to release active E2F transcription factors, which promotes entry into S phase. [Pg.341]

The activated CDKl-cyclin B kinase finally phosphor-ylates a large number of proteins most of which are not well characterized, leading to chromosome condensation, nuclear envelope breakdown, spindle assembly, and chromosome segregation. [Pg.342]


See other pages where Cyclins is mentioned: [Pg.106]    [Pg.106]    [Pg.106]    [Pg.106]    [Pg.106]    [Pg.107]    [Pg.107]    [Pg.108]    [Pg.108]    [Pg.109]    [Pg.109]    [Pg.109]    [Pg.109]    [Pg.118]    [Pg.119]    [Pg.166]    [Pg.271]    [Pg.65]    [Pg.52]    [Pg.53]    [Pg.55]    [Pg.214]    [Pg.37]    [Pg.79]    [Pg.91]    [Pg.92]    [Pg.339]    [Pg.341]    [Pg.341]    [Pg.341]    [Pg.341]    [Pg.342]    [Pg.342]   
See also in sourсe #XX -- [ Pg.333 , Pg.334 , Pg.334 , Pg.335 ]

See also in sourсe #XX -- [ Pg.6 , Pg.9 , Pg.10 ]

See also in sourсe #XX -- [ Pg.195 ]

See also in sourсe #XX -- [ Pg.73 , Pg.101 ]

See also in sourсe #XX -- [ Pg.577 ]

See also in sourсe #XX -- [ Pg.157 ]

See also in sourсe #XX -- [ Pg.214 , Pg.215 ]

See also in sourсe #XX -- [ Pg.444 ]

See also in sourсe #XX -- [ Pg.803 ]

See also in sourсe #XX -- [ Pg.29 ]

See also in sourсe #XX -- [ Pg.439 , Pg.442 ]

See also in sourсe #XX -- [ Pg.504 ]

See also in sourсe #XX -- [ Pg.281 , Pg.429 ]

See also in sourсe #XX -- [ Pg.68 , Pg.508 ]




SEARCH



B cyclins

B-type cyclins

Bisindolymaleimides cyclin-dependent kinase

CDC2-Cyclin B complex

CDKs CDK2 (cyclin

CDKs CDK7 (cyclin

CKIs (cyclin-dependent kinase inhibitors

Cancer cyclin-dependent protein kinases

Cell cycle cyclin

Cell cycle cyclin-dependent kinase

Cell cycle cyclin-dependent kinase inhibitors

Chlortetra cycline

Chlortetra cycline Tetracycline

Cyclin

Cyclin

Cyclin , mitotic

Cyclin , mitotic G1 or start

Cyclin , mitotic cell cycle

Cyclin B, degradation

Cyclin Oncogenic Activation

Cyclin Proteolytic degradation

Cyclin Stability

Cyclin Table

Cyclin box

Cyclin cell cycle regulation

Cyclin degradation

Cyclin dependent kinase

Cyclin dependent kinase 2 (Cdk

Cyclin dependent kinase inhibitors

Cyclin dependent kinase inhibitors synthesis

Cyclin destruction boxes

Cyclin during meiosis

Cyclin fold

Cyclin half-life

Cyclin kinase inhibitors

Cyclin phosphorylation

Cyclin, regulatory subunit

Cyclin, ubiquitination

Cyclin-dependant kinase inhibitor

Cyclin-dependant kinases

Cyclin-dependant kinases kinase activation

Cyclin-dependent

Cyclin-dependent kinase 2, inhibition

Cyclin-dependent kinase 4 , inhibitor activity against

Cyclin-dependent kinase cell cycle regulation

Cyclin-dependent kinase drug response

Cyclin-dependent kinase gene expression profiling

Cyclin-dependent kinase inhibitor p21Wafl

Cyclin-dependent kinase inhibitors cell cycle regulation

Cyclin-dependent kinases (Cdks

Cyclin-dependent kinases Drosophila

Cyclin-dependent kinases Xenopus

Cyclin-dependent kinases humans

Cyclin-dependent kinases mouse

Cyclin-dependent protein

Cyclin-dependent protein kinases

Cyclin-dependent protein kinases (CDK

Cyclin-dependent protein kinases (CDKs

Cyclin-dependent protein kinases (CDKs change

Cyclin-dependent protein kinases (CDKs domains

Cyclin-dependent, Mitogen-activated

Cycline-dependent kinases

Cyclins cyclin

Cyclins cyclin

Cyclins, mitotic

Cyclins, mitotic cell cycle

Cyclins, resveratrol inhibition

Cyclins/cyclin-dependent kinases

D cyclins

D-type cycline

E cyclins

Enzymes cyclin kinase

Function of the D Type Cyclins

Gl cyclin

Histone kinases cyclin-dependent kinase

M phase cyclin

Oxytetra cycline

P34 and cyclins

Promoters Cyclin

Protein inhibit cyclin-dependent kinase

Stability of Cyclins

Tetra cycline

Tumor suppressor genes cyclin dependent kinase inhibitors

Xenopus cyclin response

© 2024 chempedia.info