Intrinsically Disordered Protein: Difference between revisions

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== Many IUPs undergo disorder-order transition ==
== Many IUPs undergo disorder-order transition ==


Binding of natural ligands such as a variety of small molecules, substrates, cofactors, other proteins, nucleic acids or membranes induce folding of the unstructured protein. See the following two examples and also the page on  [http://www.proteopedia.org/wiki/index.php/Lac_repressor Lac repressor]
Binding of natural ligands such as a variety of small molecules, substrates, cofactors, other proteins, nucleic acids or membranes induces folding of unstructured proteins. See the following two examples and also the page on  [http://www.proteopedia.org/wiki/index.php/Lac_repressor Lac repressor]
 
 


=== 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> ===


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]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Tzviya Zeev-Ben-Mordehai, Eric Martz, Jaime Prilusky, Eran Hodis, Wayne Decatur, Joel L. Sussman, Karl Oberholser, David Canner, Alexander Berchansky, Michal Harel