The 2Å resolution crystal structure of HetL, a pentapeptide repeat protein involved in regulation of heterocyst differentiation in the cyanobacterium Nostoc sp. strain PCC 7120

2009 ◽  
Vol 165 (1) ◽  
pp. 47-52 ◽  
Author(s):  
S NI ◽  
G SHELDRICK ◽  
M BENNING ◽  
M KENNEDY
2014 ◽  
Vol 70 (3) ◽  
pp. 780-788 ◽  
Author(s):  
Jae-Woo Ahn ◽  
Sangwoo Kim ◽  
Eun-Jung Kim ◽  
Yeo-Jin Kim ◽  
Kyung-Jin Kim

The hPrp19–CDC5L complex plays a crucial role during human pre-mRNA splicing by catalytic activation of the spliceosome. In order to elucidate the molecular architecture of the hPrp19–CDC5L complex, the crystal structure of CTNNBL1, one of the major components of this complex, was determined. Unlike canonical ARM-repeat proteins such as β-catenin and importin-α, CTNNBL1 was found to contain a twisted and extended ARM-repeat structure at the C-terminal domain and, more importantly, the protein formed a stable dimer. A highly negatively charged patch formed in the N-terminal ARM-repeat domain of CTNNBL1 provides a binding site for CDC5L, a binding partner of the protein in the hPrp19–CDC5L complex, and these two proteins form a complex with a stoichiometry of 2:2. These findings not only present the crystal structure of a novel ARM-repeat protein, CTNNBL1, but also provide insights into the detailed molecular architecture of the hPrp19–CDC5L complex.


2009 ◽  
Vol 13 (10) ◽  
pp. 2673-2684 ◽  
Author(s):  
Zhihong Cheng ◽  
Yuying Liu ◽  
Chernhoe Wang ◽  
Roy Parker ◽  
Haiwei Song

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