Bateman domains and adenosine derivatives form a binding contract

J Clin Invest. 2004 Jan;113(2):182-4. doi: 10.1172/JCI20846.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review
  • Comment

MeSH terms

  • AMP-Activated Protein Kinases
  • Adenosine Monophosphate / chemistry
  • Adenosine Triphosphate / chemistry*
  • Amino Acid Motifs
  • Animals
  • Chlorine / chemistry
  • Cystathionine beta-Synthase / chemistry*
  • Humans
  • IMP Dehydrogenase / chemistry*
  • Immunosuppressive Agents / pharmacology
  • Models, Molecular
  • Multienzyme Complexes / chemistry
  • Mutation
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases / chemistry

Substances

  • Immunosuppressive Agents
  • Multienzyme Complexes
  • Adenosine Monophosphate
  • Chlorine
  • Adenosine Triphosphate
  • IMP Dehydrogenase
  • Protein-Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Cystathionine beta-Synthase