Bateman domains and adenosine derivatives form a binding contract.
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.
Kemp
Bruce E
BE
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia. kemp@ariel.unimelb.edu.au
D055372:AMP-Activated Protein Kinases; D000249:Adenosine Monophosphate / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry*; D020816:Amino Acid Motifs; D000818:Animals; D002713:Chlorine / Q000737:chemistry; D003541:Cystathionine beta-Synthase / Q000737:chemistry*; D006801:Humans; D007168:IMP Dehydrogenase / Q000737:chemistry*; D007166:Immunosuppressive Agents / Q000494:pharmacology; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry; D009154:Mutation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry; D017434:Protein Structure, Tertiary
D007166:Immunosuppressive Agents; D009097:Multienzyme Complexes; D000249:Adenosine Monophosphate; D002713:Chlorine; D000255:Adenosine Triphosphate; D007168:IMP Dehydrogenase; D017346:Protein Serine-Threonine Kinases; D055372:AMP-Activated Protein Kinases; D003541:Cystathionine beta-Synthase