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Updated: Jul 20, 2026
08:09
Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
Published on: January 7, 2017
Bateman domains and adenosine derivatives form a binding contract.
1St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia. kemp@ariel.unimelb.edu.au
The Journal of Clinical Investigation
|January 15, 2004
Summary
Bateman domains, formed by cystathionine beta-synthase (CBS) motifs, bind adenosyl compounds. This regulates key enzymes and channels, offering new therapeutic targets for metabolic diseases, cancer, and more.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Conserved cystathionine beta-synthase (CBS) sequence motifs form Bateman domains in various proteins.
- Understanding the function of Bateman domains is crucial for deciphering cellular regulation.
Purpose of the Study:
- To investigate the binding properties and regulatory roles of Bateman domains.
- To elucidate the connection between CBS mutations, Bateman domains, and hereditary diseases.
Main Methods:
- Bioinformatic analysis of conserved CBS motifs.
- Biochemical assays to determine adenosyl compound binding.
- Enzyme activity assays for regulated proteins.
Main Results:
- Bateman domains were confirmed to bind adenosyl compounds.
- Regulation of IMP dehydrogenase, CBS, chloride channels, and AMP-activated protein kinase by Bateman domains was established.
- A link between CBS sequence mutations and hereditary diseases was revealed.
Conclusions:
- Bateman domains are key regulators of critical cellular pathways through adenosyl compound binding.
- This discovery opens avenues for novel therapeutic strategies targeting metabolic disorders, cancer, and infectious diseases.
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