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The CBS Domain: A Protein Module with an Emerging Prominent Role in Regulation

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A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia
Department of Biochemistry and Food Chemistry, University of Turku, Turku FIN-20014, Finland
Cite this: ACS Chem. Biol. 2011, 6, 11, 1156–1163
Publication Date (Web):September 29, 2011
https://doi.org/10.1021/cb200231c
Copyright © 2011 American Chemical Society

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    Abstract

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    Regulatory CBS (cystathionine β-synthase) domains exist as two or four tandem copies in thousands of cytosolic and membrane-associated proteins from all kingdoms of life. Mutations in the CBS domains of human enzymes and membrane channels are associated with an array of hereditary diseases. Four CBS domains encoded within a single polypeptide or two identical polypeptides (each having a pair of CBS domains at the subunit interface) form a highly conserved disk-like structure. CBS domains act as autoinhibitory regulatory units in some proteins and activate or further inhibit protein function upon binding to adenosine nucleotides (AMP, ADP, ATP, S-adenosyl methionine, NAD, diadenosine polyphosphates). As a result of the differential effects of the nucleotides, CBS domain-containing proteins can sense cell energy levels. Significant conformational changes are induced in CBS domains by bound ligands, highlighting the structural basis for their effects.

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