Intrinsically Disordered Protein: Difference between revisions
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=== The human p27<sup>Kip1</sup> kinase inhibitory domain <ref>PMID: 8684460</ref> === | === The human p27<sup>Kip1</sup> kinase inhibitory domain <ref>PMID: 8684460</ref> === | ||
<applet load='1jsu' size='300' frame='true' align='right' caption='Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex (1jsu)' /> | |||
The cyclin-dependent kinases (CDKs) have a central role in coordinating the eukaryotic cell division cycle. CDKs are controlled through several different processes involving the binding of activating cyclin subunits. Complexes of cyclins with CDKs play a central role in the control of the eukaryotic cell cycle. These complexes are inhibited by other proteins termed in general cyclin-CDK inhibitors (CKIs). One example of CKIs is p27<sup>Kip1</sup>. p27<sup>Kip1</sup> is an IUP and it binds to phosphorylated <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Complex/2'>cyclin/CDK complex</scene> in <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Extended/2'>an extended conformation</scene> interacting with both <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Cyca/2'>cyclin A</scene> and <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Cdk2/3'>CDK2</scene>. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On CDK2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP. [[http://www.proteopedia.org/wiki/index.php/1jsu]] | The cyclin-dependent kinases (CDKs) have a central role in coordinating the eukaryotic cell division cycle. CDKs are controlled through several different processes involving the binding of activating cyclin subunits. Complexes of cyclins with CDKs play a central role in the control of the eukaryotic cell cycle. These complexes are inhibited by other proteins termed in general cyclin-CDK inhibitors (CKIs). One example of CKIs is p27<sup>Kip1</sup>. p27<sup>Kip1</sup> is an IUP and it binds to phosphorylated <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Complex/2'>cyclin/CDK complex</scene> in <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Extended/2'>an extended conformation</scene> interacting with both <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Cyca/2'>cyclin A</scene> and <scene name='User:Tzviya_Zeev-Ben-Mordehai/Sandbox_1/Cdk2/3'>CDK2</scene>. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On CDK2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP. [[http://www.proteopedia.org/wiki/index.php/1jsu]] | ||
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=== The transcriptional activator GCN4 <ref>PMID: 8377181</ref>=== | === The transcriptional activator GCN4 <ref>PMID: 8377181</ref>=== | ||
<applet load='1stp' size='300' frame='true' align='right' caption='The structure of GCN4 bound to a DNA fragment (1dgc) containing the perfectly symmetrical binding site. A homodimer of parallel alpha-helices form an interhelix coiled-coil region via the leucine zipper, and the two N-terminal basic regions fit into the major groove of half sites on opposite sides of the DNA double helix. Arginine and Lysines shown in sticks representation.' scene='Intrinsically_Disordered_Protein/Gcn4/1'/> | |||
The yeast transcriptional activator GCN4 belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. All family members have a DNA recognition motif consists of a coiled-coil dimerization element, the leucine-zipper, and an adjoining basic region, which mediates DNA binding. This basic region is largely unstructured in the absence of DNA, addition of DNA containing a GCN4 binding site induce the transition of this region from unstructured to α-helical. | The yeast transcriptional activator GCN4 belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. All family members have a DNA recognition motif consists of a coiled-coil dimerization element, the leucine-zipper, and an adjoining basic region, which mediates DNA binding. This basic region is largely unstructured in the absence of DNA, addition of DNA containing a GCN4 binding site induce the transition of this region from unstructured to α-helical. | ||
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== References and Notes == | == References and Notes == | ||