Key result
Deletion of the pleckstrin homology domain (residues 116-232) of the p130 protein completely abolished Ins(1,4,5)P3 binding activity, with the 4,5-vicinal phosphate pair being essential for binding.
Population
COS-1 cells and bacterial expression system expressing a novel 130 kDa protein (p130) or its truncated mutants
Design
Preclinical
Authors
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Defines p130 PH domain requirements for InsP3 binding; leaves open its role in cardiovascular signaling pathways.
The pleckstrin homology domain of the novel 130 kDa protein is the specific binding site for Ins(1,4,5)P3 and Ins(1,4,5,6)P4, exhibiting unique structural determinants for ligand specificity.
Takeuchi et al. (1996) studied this question. p130 protein PH domain mutants was evaluated on Binding activity of Ins(1,4,5)P3 and Ins(1,4,5,6)P4. Deletion of the pleckstrin homology domain (residues 116-232) of the p130 protein completely abolished Ins(1,4,5)P3 binding activity, with the 4,5-vicinal phosphate pair being essential for binding.
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