title: CBS domains: Ligand binding sites and conformational variability.
abstract: Cystathionine β-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.
authors.affiliation: Structural Biology Unit, CIC bioGUNE, Technological Park of Bizkaia, Ed. 800, 48160 Derio, Bizkaia, Spain.
authors.forename: June
authors.initials: J
authors.lastname: Ereño-Orbea
authors.forename: Iker
authors.initials: I
authors.lastname: Oyenarte
authors.forename: Luis Alfonso
authors.initials: LA
authors.lastname: Martínez-Cruz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003541:Cystathionine beta-Synthase / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
chemical_list: D008024:Ligands; D003541:Cystathionine beta-Synthase
keywords: Adenosine; Bateman module; CBS module; CBS motif; DNA; Metal ions; Nucleotide