|PROSITE documentation PDOC51371 [for PROSITE entry PS51371]|
CBS domains contain about 60 amino acid residues and occur as tandem pairs in a variety of proteins in bacteria, archaea, and eukaryotes [1,2]. They are mainly found in proteins that are regulated by adenosyl metabolites. Depending on the protein in which they occur, CBS domains have been proposed to affect multimerization and sorting of proteins, channel gating, and ligand binding. However, recent experiments revealing that CBS domains can bind adenosine-containing ligands such ATP, AMP, or S-adenosylmethionine have led to the hypothesis that CBS domains function as sensors of intracellular metabolites [3,4].
Crystallographic studies of CBS domains have shown that pairs of CBS sequences form a globular domain where each CBS unit adopts a β-α-β-β-α pattern (see <PDB:1ZFJ>) . Crystal structure of the CBS domains of the AMP-activated protein kinase in complexes with AMP and ATP shows that the phosphate groups of AMP/ATP lie in a surface pocket at the interface of two CBS domains, which is lined with basic residues, many of which are associated with disease-causing mutations .
Some proteins known to contain a CBS domain:
The profile we developed covers the entire CBS domain.Note:
Each pair of CBS motifs is also known as a Bateman domain .Last update:
February 2008 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||The structure of a domain common to archaebacteria and the homocystinuria disease protein.|
|Source||Trends Biochem. Sci. 22:12-13(1997).|
|2||Authors||Ignoul S., Eggermont J.|
|Title||CBS domains: structure, function, and pathology in human proteins.|
|Source||Am. J. Physiol. 289:C1369-C1378(2005).|
|3||Authors||Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G.|
|Title||CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations.|
|Source||J. Clin. Invest. 113:274-284(2004).|
|Title||Bateman domains and adenosine derivatives form a binding contract.|
|Source||J. Clin. Invest. 113:182-184(2004).|
|5||Authors||Zhang R., Evans G., Rotella F.J., Westbrook E.M., Beno D., Huberman E., Joachimiak A., Collart F.R.|
|Title||Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.|
|6||Authors||Xiao B., Heath R., Saiu P., Leiper F.C., Leone P., Jing C., Walker P.A., Haire L., Eccleston J.F., Davis C.T., Martin S.R., Carling D., Gamblin S.J.|
|Title||Structural basis for AMP binding to mammalian AMP-activated protein kinase.|