Phospholipase C
FunctionPhospholipase C (PLC) cleaves phospholipids before the phosphate group. PLCs catalyze the conversion of phosphatidylinositol 4,5-bisphosphate to inositol 1,4,5-trisphosphate and diacylglycerol.[1]
DiseasePhospholipase C γ gene blocking can stop breast cancer.[5] Phospholipase C δ has important suppressive role in the development and progression of esophageal carcinoma. Mutations in phospholipase C δ1 cause hereditary leukonychia[6]. Mutations in phospholipase C ε1 are associated with stomach cancer risk and nephrotic syndromes[7]. Structural highlightsThe active site of PIPLC is located at a solvent-accessible cleft at the C-terminal.[8] Solvent-accessible cleft.
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3D structures of phospholipase C
Updated on 11-May-2026
- PIPLC
- PLC beta 3 Gq – BcPIPLC – Bacillus cereus
- IP3 is second messenger, 3ptd, 4ptd, 5ptd, 6ptd, 7ptd – BcPIPLC (mutant)
- 2plc – LmPIPLC – Listeria monocytogenes
- 3ea1 – BtPIPLC – Bacillus thuringiensis
- 1t6m, 2or2, 3ea3 – BtPIPLC (mutant)
- 3v18 – SaPIPLC – Staphylococcus aureus
- 4f2t, 4f2u, 4i8y, 4i9m – SaPIPLC (mutant)
- 5fyo, 5fyp – PsPIPLC – Pseudomonas
- PLC beta 3 Gq – BcPIPLC – Bacillus cereus
- PIPLC complex
- 1ptg – BcPIPLC + myo-inositol
- 1gym – BcPIPLC + glucosamine-myo-inositol
- 1aod – LmPIPLC + myo-inositol
- 3ea2 – BtPIPLC + myo-inositol
- 5fyr – PsPIPLC + myo-inositol
- 3v16, 4f2b, 4rv3 – SaPIPLC + myo-inositol
- 3v1h, 4i9t, 4s3g – SaPIPLC (mutant) + myo-inositol
- 4i90 – SaPIPLC (mutant) + choline
- 4i9j – SaPIPLC (mutant) + diC4PC
- 1ptg – BcPIPLC + myo-inositol
- Phospholipase C β
- 2zkm – hPLCB-2 - human
- 2fju – hPLCB-2 + RAC1
- 8emv – hPLCB-3 – Cryo EM
- 7sq2, 4gnk, 4qj3 – hPLCB-3 + guanine nucleotide-binding protein G subunit alpha
- 4qj4, 4qj5 – hPLCB-3 + guanine nucleotide-binding protein G subunit alpha + inositol phosphate derivative
- 7sq2 – hPLCB-3 + guanine nucleotide-binding protein G subunit alpha + GDP
- 8emw, 8emx – hPLCB-3 + guanine nucleotide-binding protein G subunits beta+gamma – Cryo EM
- 1jad – PLCB - turkey
- 3qr0 – PLCB - cuttlefish
- 3qr1 – PLCB - squid
- 2zkm – hPLCB-2 - human
- Phospholipase C γ
- 1hsq, 2hsp – hPLCG SH3 domain - NMR
- 4fbn – hPLCG-1
- 2k2j – hPLCG-2 split PH2 domain - NMR
- 2w2w – hPLCG-2 split PH2 domain (mutant)
- 2w2x – hPLCG-2 split PH2 domain + RAC2 br />
- 4ey0 – hPLCG-1 SH2 domain (mutant)
- 7nxe – hPLCG-1 SH2 domain + peptide
- 2pld, 2ple – PLCG C terminal SH2 domain + PDGF peptide – bovine - NMR
- 6pbc – rPLCG-1 – rat
- 1ywp – rPLCG-1 SH3 domain 790-851
- 1y0m – rPLCG-1 SH3 domain (mutant)
- 2fjl – rPLCG-1 split PH2 domain - NMR
- 2eob – rPLCG-2 SH2 domain 633-743 - NMR
- 1ywo – rPLCG-1 SH3 domain + lymphocyte cytosolic protein peptide
- 7z3j – rPLCG-1 + inositol-3P
- 4k44, 4k45 – rPLCG C terminal SH2 domain
- 2dx0 – mPLCG-2 N terminal SH2 domain – mouse
- 2eqi – mPLCG-2 SH3 domain - NMR
- 1hsq, 2hsp – hPLCG SH3 domain - NMR
- Phospholipase C δ
- Phospholipase C ε
- Phospholipase C
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman