Domain
CBS domain (IPR000644)
Short name:
CBS_dom
Overlapping homologous superfamilies
None.
Domain relationships
None.
Description
CBS domains are small intracellular modules that pair together to form a stable globular domain [PMID: 10200156]. Pairs of these domains have been termed a Bateman domain [PMID: 14722609]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [PMID: 14722619]. 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 [PMID: 11524006]. CBS domain pairs from AMPK bind AMP or ATP [PMID: 14722619]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [PMID: 14722619].
Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR.
Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.
Biochemistry 38 4691-700 1999
Kemp BE.
Bateman domains and adenosine derivatives form a binding contract.
J. Clin. Invest. 113 182-4 2004
Scott JW, Hawley SA, Green KA, Anis M, Stewart G, Scullion GA, Norman DG, Hardie DG.
CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations.
J. Clin. Invest. 113 274-84 2004
Janosik M, Kery V, Gaustadnes M, Maclean KN, Kraus JP.
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 2001
Scott JW, Hawley SA, Green KA, Anis M, Stewart G, Scullion GA, Norman DG, Hardie DG.
CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations.
J. Clin. Invest. 113 274-84 2004
Scott JW, Hawley SA, Green KA, Anis M, Stewart G, Scullion GA, Norman DG, Hardie DG.
CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations.
J. Clin. Invest. 113 274-84 2004
InterPro