Summary for 2ISD
| Entry DOI | 10.2210/pdb2isd/pdb |
| Descriptor | PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1, ACETATE ION (3 entities in total) |
| Functional Keywords | phosphoric diester hydrolase, hydrolase, lipid degradation, transducer, calcium-binding, phospholipase c, phosphoinositide-specific |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 2 |
| Total formula weight | 141267.12 |
| Authors | Essen, L.-O.,Perisic, O.,Williams, R.L. (deposition date: 1997-03-31, release date: 1997-07-07, Last modification date: 2024-02-21) |
| Primary citation | Essen, L.O.,Perisic, O.,Cheung, R.,Katan, M.,Williams, R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature, 380:595-602, 1996 Cited by PubMed Abstract: Mammalian phosphoinositide-specific phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The 2.4-A structure of phospholipase C delta 1 reveals a multidomain protein incorporating modules shared by many signalling proteins. The structure suggests a mechanism for membrane attachment and Ca2+-dependent hydrolysis of second-messenger precursors. The regulation and reversible membrane association of PI-PLC may serve as a model for understanding other multidomain enzymes involved in phospholipid signalling. PubMed: 8602259DOI: 10.1038/380595a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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