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The KIND module: a putative signalling domain evolved from the C lobe of the protein kinase fold

Official URL:https://doi.org/10.1016/S0968-0004(03)00116-6
PubMed:View item in PubMed
Creators Name:Ciccarelli, F.D. and Bork, P. and Kerkhoff, E.
Journal Title:Trends in Biochemical Sciences
Journal Abbreviation:Trends Biochem Sci
Volume:28
Number:7
Page Range:349-352
Date:7 July 2003
Keywords:Amino Acid Sequence, Amino Acid Sequence Homology, Molecular Models, Molecular Sequence Data, Protein Binding, Protein Conformation, Protein Kinases, Sequence Alignment, Signal Transduction, Tertiary Protein Structure, Animals
Abstract:A novel putative interaction domain - KIND (kinase non-catalytic C-lobe domain) - has been identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of the novel domain only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features.
ISSN:0968-0004
Publisher:Elsevier (The Netherlands)
Item Type:Article

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