PDB ID or protein name

1mai » PH domain of phospholipase C delta 1

1mai » PH domain of phospholipase C delta 1
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Topology in Eukaryotic plasma membrane
Topologyextracellular side
cytoplasmic side
1mai » PH domain of phospholipase C delta 1
Depth 15.0 ± 1.8 Å
Tilt Angle 22 ± 14°
ΔGtransfer -17.8 kcal/mol
Links to 1mai PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology cytoplasmic
Resolution 1.90 Å
Other PDB entries representing this structure none
Number of subunits 1
Experimental Verification for 1mai » PH domain of phospholipase C delta 1
This position was calculated for the complex with bound lipid. Lipid acyl chains were modelled. Calculated hydrocarbon boundary of the lipid bilayer corresponds to the carbonyl groups of the bound lipid. Spatial positions of the protein calculated with and without the bound lipid are almost identical. Transfer energy was calculated without contribution from the bound lipid. Experimental membrane binding affinity is -6.2 kcal/mol in the presence of PIP2 and less than -4 kcal/mol without PIP2 (Wang et al. 1999).
2 references
Singh SM, Murray D. 2003. Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains. Protein Sci. 12:1934-53. PubMed
Wang T, Pentyala S, Rebecchi MJ, Scarlata S. 1999. Differential association of the pleckstrin homology domains of phospholipases C-beta 1, C-beta 2, and C-delta 1 with lipid bilayers and the beta gamma subunits of heterotrimeric G proteins. Biochemistry 38:1517-24. PubMed
Comments on 1mai » PH domain of phospholipase C delta 1
This orientation is in agreement with results of computational modeling based on electrostatic interactions (Singh and Murray 2003). However, PH domain penetrates by ~15A deeper into the membrane according to our results: nonpolar residues are inserted in the membrane hydrocarbon core, not in the head group region.