| Literature DB >> 21187076 |
Wen Zhang1, Jiahai Zhang, Xuecheng Zhang, Chao Xu, Xiaoming Tu.
Abstract
Rap1 (repressor-activator protein 1) from Saccharomyces cerevisiae, containing a BRCT domain at its N-terminus, is a multifunctional protein that controls telomere function, silencing, and the activation of glycolytic and ribosomal protein genes. In this work, we determined the solution structure of Rap1 BRCT domain, which contains three β-strands and three α-helices. Structural comparison indicated that Rap1 BRCT domain adopts a global fold similar to other BRCT domains, implying some common structural aspects of BRCT domain family. On the other hand, Rap1 BRCT domain displays structural characteristics significantly different from other BRCT domains in that Rap1 BRCT domain adopts a rather flexible conformation with less secondary structure elements, revealing a novel fold of the BRCT domain family. CrownEntities:
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Year: 2010 PMID： 21187076 DOI： 10.1016/j.bbrc.2010.12.109
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575