3brv: Difference between revisions

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[[Image:3brv.~~jpg~~|left|200px]]

[[Image:3brv.png|left|200px]]

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~~'''~~NEMO/IKKb association domain structure~~'''~~

===NEMO/IKKb association domain structure===

~~==Overview==~~

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The ~~phosphorylation of IkappaB by~~ the ~~IKK complex targets it for degradation and releases NF-kappaB for translocation into the nucleus~~ to ~~initiate~~ the ~~inflammatory response, cell proliferation, or cell differentiation. The IKK complex is composed of the catalytic IKKalpha~~/~~beta kinases and a regulatory protein, NF-kappaB essential modulator (NEMO; IKKgamma)~~. ~~NEMO associates with the unphosphorylated IKK kinase C termini and activates the IKK complex's catalytic activity~~. ~~However~~, ~~detailed structural information about the NEMO/IKK interaction~~ is ~~lacking. In this study, we have identified the minimal requirements for NEMO and IKK kinase association using a variety of biophysical techniques and have solved two crystal structures of~~ the minimal NEMO/IKK kinase associating domains. We demonstrate that the NEMO core domain is a dimer that binds two IKK fragments and identify energetic hot spots that can be exploited to inhibit IKK complex formation with a therapeutic agent.

The line below this paragraph, {{ABSTRACT_PUBMED_18462684}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18462684 is the PubMed ID number.

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==About this Structure==

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[[Category: Transferase]]

[[Category: Transferase/transcription complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu May 22 22~~:35:37 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:26:07 2008''

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-[[Image:3brv.jpg|left|200px]]
+{{Seed}}
+[[Image:3brv.png|left|200px]]
 <!--
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 {{STRUCTURE_3brv|  PDB=3brv  |  SCENE=  }}
-'''NEMO/IKKb association domain structure'''
+===NEMO/IKKb association domain structure===
-==Overview==
+<!--
-The phosphorylation of IkappaB by the IKK complex targets it for degradation and releases NF-kappaB for translocation into the nucleus to initiate the inflammatory response, cell proliferation, or cell differentiation. The IKK complex is composed of the catalytic IKKalpha/beta kinases and a regulatory protein, NF-kappaB essential modulator (NEMO; IKKgamma). NEMO associates with the unphosphorylated IKK kinase C termini and activates the IKK complex's catalytic activity. However, detailed structural information about the NEMO/IKK interaction is lacking. In this study, we have identified the minimal requirements for NEMO and IKK kinase association using a variety of biophysical techniques and have solved two crystal structures of the minimal NEMO/IKK kinase associating domains. We demonstrate that the NEMO core domain is a dimer that binds two IKK fragments and identify energetic hot spots that can be exploited to inhibit IKK complex formation with a therapeutic agent.
+The line below this paragraph, {{ABSTRACT_PUBMED_18462684}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18462684 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18462684}}
 ==About this Structure==
@@ Line 46: / Line 50: @@
 [[Category: Transferase]]
 [[Category: Transferase/transcription complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:35:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:26:07 2008''