C2 domain conformational changes in phospholipase C-δ1
- 1 September 1996
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 3 (9) , 788-795
- https://doi.org/10.1038/nsb0996-788
Abstract
The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-delta 1 has been determined at 2.4 A resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical. The Ca2+ analogue Sm3+ binds at two sites between the jaws of the C2 domain. Sm3+ binding ejects three lysine residues which bridge the gap between the jaws and occupy the Ca2+ site in the apoenzyme, triggering a conformational change in the jaws. The distal sections of the C2 jaws move apart, opening the mouth by 9 A and creating a gap large enough to bind a phospholipid headgroup.Keywords
This publication has 34 references indexed in Scilit:
- Crystal structure of a mammalian phosphoinositide-specific phospholipase CδNature, 1996
- Extending the C2 domain family: C2s in PKCs δ, ϵ,η,θ, phospholipases, GAPs, and perforinProtein Science, 1996
- Significance of PIP2 hydrolysis and regulation of phospholipase C isozymesCurrent Opinion in Cell Biology, 1995
- Phospholipase C δ1 requires a pleckstrin homology domain for interaction with the plasma membraneBiochemical Journal, 1995
- The pleckstrin homology domain of phospholipase C-.delta.1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranesBiochemistry, 1995
- Protein Kinase C: Seeing two domainsCurrent Biology, 1995
- Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptorNature, 1995
- Crystal Structure of the Mammalian Grb2 AdaptorScience, 1995
- Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding foldCell, 1995
- Structure of the regulatory domains of the Src-family tyrosine kinase LckNature, 1994