InterPro domain: IPR000644

CBS domains are small intracellular modules that pair together to form a stable globular domain [ 1 ]. Pairs of these domains have been termed a Bateman domain [ 2 ]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [ 3 ]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in cystathionine-beta synthase is involved in regulation by S-AdoMet [ 4 ]. CBS domain pairs from AMPK bind AMP or ATP [ 5 ]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [ 5 ].

1. Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. Biochemistry 38, 4691-700
2. Bateman domains and adenosine derivatives form a binding contract. J. Clin. Invest. 113, 182-4
3. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 113, 274-84
4. Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. Biochemistry 40, 10625-33