Bateman domains and adenosine derivatives form a binding contract
- PMID: 14722609
- PMCID: PMC311445
- DOI: 10.1172/JCI20846
Bateman domains and adenosine derivatives form a binding contract
Abstract
Conserved pairs of CBS sequence motifs (named after cystathionine beta-synthase) found in a wide variety of proteins associate to form Bateman domains. A new study establishes that Bateman domains bind adenosyl compounds and regulate IMP dehydrogenase, CBS, chloride channels, and AMP-activated protein kinase. This discovery reveals how mutations in CBS sequences in these proteins cause hereditary diseases and provides a rich vista of conceptual opportunities for therapies in energy metabolism, obesity, diabetes, cancer, antivirals, and immunosuppression.
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Comment on
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CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations.J Clin Invest. 2004 Jan;113(2):274-84. doi: 10.1172/JCI19874. J Clin Invest. 2004. PMID: 14722619 Free PMC article.
References
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- The CBS domain web page. The Sanger Institute. http://www.sanger.ac.uk/Users/agb/CBS/CBS.html.
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- Bateman A. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem. Sci. 1997;22:12–13. - PubMed
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- Zhang R, et al. Characteristics and crystal structure of bacterial inosine-5′-monophosphate dehydrogenase. Biochemistry. 1999;38:4691–4700. - PubMed
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