1k1a
From Proteopedia
|
Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family
Contents |
Overview
IkappaB proteins associate with the transcription factor NF-kappaB via, their ankyrin repeat domain. Bcl-3 is an unusual IkappaB protein because, it is primarily nucleoplasmic and can lead to enhanced NF-kappaB-dependent, transcription, unlike the prototypical IkappaB protein IkappaBalpha, which, inhibits NF-kappaB activity by retaining it in the cytoplasm. Here we, report the 1.9 A crystal structure of the ankyrin repeat domain of human, Bcl-3 and compare it with that of IkappaBalpha bound to NF-kappaB. The two, structures are highly similar over the central ankyrin repeats but differ, in the N-terminal repeat and at the C-terminus, where Bcl-3 contains a, seventh repeat in place of the acidic PEST region of IkappaBalpha., Differences between the two structures suggest why Bcl-3 differs from, IkappaBalpha in selectivity towards various NF-kappaB species, why Bcl-3, but not IkappaBalpha can associate with its NF-kappaB partner bound to, DNA, and why two molecules of Bcl-3 but only one of IkappaBalpha can bind, to its NF-kappaB partner. Comparison of the two structures thus provides, an insight into the functional diversity of IkappaB proteins.
Disease
Known disease associated with this structure: Leukemia/lymphoma, B-cell OMIM:[109560]
About this Structure
1K1A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family., Michel F, Soler-Lopez M, Petosa C, Cramer P, Siebenlist U, Muller CW, EMBO J. 2001 Nov 15;20(22):6180-90. PMID:11707390
Page seeded by OCA on Mon Nov 12 17:46:24 2007
