期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 540, 期 1-2, 页码 70-81出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2013.10.008
关键词
CBS motif; Bateman module; CBS module; Adenosine; Nucleotide; Metal ions; DNA
资金
- Departamento de Educacion, Universidades e Investigacion del Gobierno Vasco [PI2010-17]
- Departamento de Industria, Innovacion, Comercio y Turismo del Gobierno Vasco [ETORTEK IE05-147, IE07-202]
- Diputacion Foral de Bizkaia [7/13/08/2006/11, 7/13/08/2005/14]
- Spanish Ministerio de Ciencia e Innovacion (MICINN) [BFU2010-17857]
- MICINN CONSOLIDER-INGENIO Program [CSD2008-00005]
Cystathionine B-synthase (CBS) domains or CBS motifs are conserved structural domains that are present in thousands of non functionally-related proteins from all kingdoms of life. Their importance is underlined by the range of hereditary diseases associated with mutations in their amino acid sequence. CBS motifs associate in pairs referred to as Bateman modules. In contrast with initial assumptions, it is now well documented that CBS motifs and/or Bateman modules may suffer conformational changes upon binding of adenosine derivatives, metal ions or nucleic acids. The degree and direction of these structural changes depend on the type of ligand, the intrinsic features of the binding sites and the association manner of the Bateman modules. This review aims to provide a summary of the current knowledge on the structural basis of ligand recognition and on the structural effects caused by these ligands in CBS domain containing proteins. (C) 2013 Elsevier Inc. All rights reserved.
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