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

TY - JOUR

T1 - The KIND module

T2 - a putative signalling domain evolved from the C lobe of the protein kinase fold

AU - Ciccarelli, F. D.

AU - Bork, P.

AU - Kerkhoff, E.

PY - 2003/7/1

Y1 - 2003/7/1

N2 - 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.

AB - 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.

KW - Ciccarelli

U2 - 10.1016/S0968-0004(03)00116-6

DO - 10.1016/S0968-0004(03)00116-6

M3 - Article

SN - 0968-0004

VL - 28

SP - 349

EP - 352

JO - TRENDS IN BIOCHEMICAL SCIENCES

JF - TRENDS IN BIOCHEMICAL SCIENCES

IS - 7

M1 - N/A

ER -