Mechanism of CDK5/p25 binding by CDK inhibitors
Identifieur interne : 000731 ( PascalFrancis/Curation ); précédent : 000730; suivant : 000732Mechanism of CDK5/p25 binding by CDK inhibitors
Auteurs : Marina Mapelli [Italie] ; Lucia Massimiliano [Italie] ; Claudia Crovace [Italie, États-Unis] ; Markus A. Seeliger [États-Unis] ; Li-Huei Tsai [France] ; Laurent Meijer [France] ; Andrea Musacchio [Italie]Source :
- Journal of medicinal chemistry : (Print) [ 0022-2623 ] ; 2005.
Descripteurs français
- Pascal (Inist)
- Activité biologique, Transduction signal, Inhibiteur enzyme, Protein kinase, Mécanisme action, Modèle moléculaire, Structure cristalline, Complexe enzyme inhibiteur, Purine dérivé, Indole dérivé, Oxime, Inhibiteur cdk5, Purine(6-benzylamino-2-[1-(hydroxyméthyl)propylamino]-9-isopropyl), Pyrrolo[2,3-b]pyrazine dérivé, Pyrrolopyrazine, Aloisine A, Indirubine oxime.
English descriptors
- KwdEn :
Abstract
The cyclin-dependent kinases (CDK) CDK1, CDK2, CDK4, and CDK6 are serine/threonine protein kinases targeted in cancer therapy due to their role in cell cycle progression. The postmitotic CDK5 is involved in biological pathways important for neuronal migration and differentiation. CDK5 represents an attractive pharmacological target as its deregulation is implicated in various neurodegenerative diseases such as Alzheimer's, Parkinson's, and Niemann-Pick type C diseases, ischemia, and amyotrophic lateral sclerosis. We have generated an improved crystal form of CDK5 in complex with p25, a segment of the p35 neuronal activator. The crystals were used to solve the structure of CDK5/p25 with (R)-roscovitine and aloisine at a resolution of 2.2 and 2.3 Å, respectively. The structure of CDK5/p25/roscovitine provides a rationale for the preference of CDK5 for the R over the S stereoisomer. Furthermore, roscovitine stabilized an unusual collapsed conformation of the glycine-rich loop, an important site of CDK regulation, and we report an investigation of the effects of glycine-rich loop phosphorylation on roscovitine binding. The CDK5/p25 crystals represent a valuable new tool for the identification and optimization of selective CDK inhibitors.
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<front><div type="abstract" xml:lang="en">The cyclin-dependent kinases (CDK) CDK1, CDK2, CDK4, and CDK6 are serine/threonine protein kinases targeted in cancer therapy due to their role in cell cycle progression. The postmitotic CDK5 is involved in biological pathways important for neuronal migration and differentiation. CDK5 represents an attractive pharmacological target as its deregulation is implicated in various neurodegenerative diseases such as Alzheimer's, Parkinson's, and Niemann-Pick type C diseases, ischemia, and amyotrophic lateral sclerosis. We have generated an improved crystal form of CDK5 in complex with p25, a segment of the p35 neuronal activator. The crystals were used to solve the structure of CDK5/p25 with (R)-roscovitine and aloisine at a resolution of 2.2 and 2.3 Å, respectively. The structure of CDK5/p25/roscovitine provides a rationale for the preference of CDK5 for the R over the S stereoisomer. Furthermore, roscovitine stabilized an unusual collapsed conformation of the glycine-rich loop, an important site of CDK regulation, and we report an investigation of the effects of glycine-rich loop phosphorylation on roscovitine binding. The CDK5/p25 crystals represent a valuable new tool for the identification and optimization of selective CDK inhibitors.</div>
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<s5>76</s5>
</fC03>
<fC03 i1="13" i2="X" l="FRE"><s0>Purine(6-benzylamino-2-[1-(hydroxyméthyl)propylamino]-9-isopropyl)</s0>
<s2>NK</s2>
<s4>INC</s4>
<s5>78</s5>
</fC03>
<fC03 i1="14" i2="X" l="FRE"><s0>Pyrrolo[2,3-b]pyrazine dérivé</s0>
<s2>NK</s2>
<s4>INC</s4>
<s5>79</s5>
</fC03>
<fC03 i1="15" i2="X" l="FRE"><s0>Pyrrolopyrazine</s0>
<s4>INC</s4>
<s5>80</s5>
</fC03>
<fC03 i1="16" i2="X" l="FRE"><s0>Aloisine A</s0>
<s4>INC</s4>
<s5>81</s5>
</fC03>
<fC03 i1="17" i2="X" l="FRE"><s0>Indirubine oxime</s0>
<s4>INC</s4>
<s5>83</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Transferases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Transferases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Transferases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fN21><s1>136</s1>
</fN21>
<fN44 i1="01"><s1>PSI</s1>
</fN44>
<fN82><s1>PSI</s1>
</fN82>
</pA>
</standard>
</inist>
</record>
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