2pop: Difference between revisions

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[[Image:2pop.jpg|left|200px]]
[[Image:2pop.jpg|left|200px]]


{{Structure
<!--
|PDB= 2pop |SIZE=350|CAPTION= <scene name='initialview01'>2pop</scene>, resolution 3.10&Aring;
The line below this paragraph, containing "STRUCTURE_2pop", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= MAP3K7IP1, TAB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BIRC4, API3, IAP3, XIAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=
{{STRUCTURE_2pop|  PDB=2pop |  SCENE= }}  
|RELATEDENTRY=[[2poi|2POI]], [[2pom|2POM]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pop OCA], [http://www.ebi.ac.uk/pdbsum/2pop PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pop RCSB]</span>
}}


'''The Crystal Structure of TAB1 and BIR1 complex'''
'''The Crystal Structure of TAB1 and BIR1 complex'''
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Lin, S C.]]
[[Category: Lin, S C.]]
[[Category: bir domain]]
[[Category: Bir domain]]
[[Category: pp2c-like domain]]
[[Category: Pp2c-like domain]]
[[Category: zinc finger]]
[[Category: Zinc finger]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:33:14 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:38:50 2008''

Revision as of 13:33, 4 May 2008

File:2pop.jpg

Template:STRUCTURE 2pop

The Crystal Structure of TAB1 and BIR1 complex


OverviewOverview

In addition to caspase inhibition, X-linked inhibitor of apoptosis (XIAP) induces NF-kappaB and MAP kinase activation during TGF-b and BMP receptor signaling and upon overexpression. Here we show that the BIR1 domain of XIAP, which has no previously ascribed function, directly interacts with TAB1 to induce NF-kappaB activation. TAB1 is an upstream adaptor for the activation of the kinase TAK1, which in turn couples to the NF-kappaB pathway. We report the crystal structures of BIR1, TAB1, and the BIR1/TAB1 complex. The BIR1/TAB1 structure reveals a striking butterfly-shaped dimer and the detailed interaction between BIR1 and TAB1. Structure-based mutagenesis and knockdown of TAB1 show unambiguously that the BIR1/TAB1 interaction is crucial for XIAP-induced TAK1 and NF-kappaB activation. We show that although not interacting with BIR1, Smac, the antagonist for caspase inhibition by XIAP, also inhibits the XIAP/TAB1 interaction. Disruption of BIR1 dimerization abolishes XIAP-mediated NF-kappaB activation, implicating a proximity-induced mechanism for TAK1 activation.

About this StructureAbout this Structure

2POP is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization., Lu M, Lin SC, Huang Y, Kang YJ, Rich R, Lo YC, Myszka D, Han J, Wu H, Mol Cell. 2007 Jun 8;26(5):689-702. PMID:17560374 Page seeded by OCA on Sun May 4 13:33:14 2008

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