1MAI

STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE

Summary for 1MAI

• Entry DOI: 10.2210/pdb1mai/pdb
• Descriptor: PHOSPHOLIPASE C DELTA-1, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: pleckstrin, phospholipase, inositol trisphosphate, signal transduction protein, hydrolase
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 15865.67

Authors

Ferguson, K.M.,Lemmon, M.A.,Schlessinger, J.,Sigler, P.B. (deposition date: 1996-05-23, release date: 1996-11-08, Last modification date: 2024-02-14)

Primary citation

Ferguson, K.M.,Lemmon, M.A.,Schlessinger, J.,Sigler, P.B.
Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain.
Cell(Cambridge,Mass.), 83:1037-1046, 1995

PubMed Abstract: The X-ray crystal structure of the high affinity complex between the pleckstrin homology (PH) domain from rat phospholipase C-delta 1 (PLC-delta 1) and inositol-(1,4,5)-trisphosphate (Ins(1,4,5)P3) has been refined to 1.9 A resolution. The domain fold is similar to others of known structure. Ins(1,4,5)P3 binds on the positively charged face of the electrostatically polarized domain, interacting predominantly with the beta 1/beta 2 and beta 3/beta 4 loops. The 4- and 5-phosphate groups of Ins(1,4,5)P3 interact much more extensively than the 1-phosphate. Two amino acids in the PLC-delta 1 PH domain that contact Ins(1,4,5)P3 have counterparts in the Bruton's tyrosine kinase (Btk) PH domain, where mutational changes cause inherited agammaglobulinemia, suggesting a mechanism for loss of function in Btk mutants. Using electrostatics and varying levels of head-group specificity, PH domains may localize and orient signaling proteins, providing a general membrane targeting and regulatory function.

PubMed: 8521504
DOI: 10.1016/0092-8674(95)90219-8

Experimental method

X-RAY DIFFRACTION (1.9 Å)