Crystal structure of a full-length β-catenin

被引：152

作者：

Xing, Yi ^{[1
]}

Takemaru, Ken-Ichi ^{[2
,3
,4
]}

Liu, Jing ^{[1
]}

Berndt, Jason D. ^{[2
,3
,4
]}

Zheng, Jie J. ^{[5
]}

Moon, Randall T. ^{[2
,3
,4
]}

Xu, Wenqing ^{[1
]}

机构：

[1] Univ Washington, Sch Med, Dept Biol Struct, Seattle, WA 98195 USA

[2] Univ Washington, Sch Med, Dept Pharmacol, Seattle, WA 98195 USA

[3] Univ Washington, Sch Med, Howard Hughes Med Inst, Seattle, WA 98195 USA

[4] Univ Washington, Sch Med, Inst Stem Cell & Regenerat Med, Seattle, WA 98195 USA

[5] St Jude Childrens Res Hosp, Dept Biol Struct, Memphis, TN 38105 USA

来源：

STRUCTURE | 2008年 / 16卷 / 03期

关键词：

D O I：

10.1016/j.str.2007.12.021

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

beta-catenin plays essential roles in cell adhesion and Wnt signaling, while deregulation of beta-catenin is associated with multiple diseases including cancers. Here, we report the crystal structures of full-length zebrafish beta-catenin and a human beta-catenin fragment that contains both the armadillo repeat and the C-terminal domains. Our structures reveal that the N-terminal region of the C-terminal domain, a key component of the C-terminal transactivation domain, forms a long a helix that packs on the C-terminal end of the armadillo repeat domain, and thus forms part of the beta-catenin superhelical core. The existence of this helix redefines our view of interactions of beta-catenin with some of its critical partners, including ICAT and Chibby, which may form extensive interactions with this C-terminal domain alpha helix. Our crystallographic and NMR studies also suggest that the unstructured N-terminal and C-terminal tails interact with the ordered armadillo repeat domain in a dynamic and variable manner.

引用

页码：478 / 487

页数：10