2pom: Difference between revisions

Revision as of 07:27, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2pom.png

Template:STRUCTURE 2pom

TAB1 with manganese ionTAB1 with manganese ion

Template:ABSTRACT PUBMED 17560374

About this StructureAbout this Structure

2POM is a Single protein structure of sequence 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 Tue Jul 29 07:27:06 2008

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

OCA

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-[[Image:2pom.jpg|left|200px]]
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 {{STRUCTURE_2pom|  PDB=2pom  |  SCENE=  }}
-'''TAB1 with manganese ion'''
+===TAB1 with manganese ion===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17560374}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17560374 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17560374}}
 ==About this Structure==
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 [[Category: Lin, S C.]]
 [[Category: Pp2c-like domain]]
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