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

Item Type:	Article
Title:	The KIND module: a putative signalling domain evolved from the C lobe of the protein kinase fold
Creators Name:	Ciccarelli, F.D. and Bork, P. and Kerkhoff, E.
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.
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
Source:	Trends in Biochemical Sciences
ISSN:	0968-0004
Publisher:	Elsevier
Volume:	28
Number:	7
Page Range:	349-352
Date:	7 July 2003
Official Publication:	https://doi.org/10.1016/S0968-0004(03)00116-6
PubMed:	View item in PubMed

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