Protein Family Models

CBS domains are small intracellular modules that pair together to form a stable globular domain [2]. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain [6]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [5]. 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]. Discovery and naming of the CBS domain. [1]. 9020585. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Bateman A;. Trends Biochem Sci 1997;22:12-13. 3D Structure found as a sub-domain in TIM barrel of inosine-monophosphate dehydrogenase. [2]. 10200156. Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR;. Biochemistry 1999;38:4691-4700. Discovery of CBS domain. [3]. 9106071. CBS domains in ClC chloride channels implicated in myotonia and nephrolithiasis (kidney stones). Ponting CP;. J Mol Med 1997;75:160-163. [4]. 11524006. 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. Janosik M, Kery V, Gaustadnes M, Macl. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16