1mai
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(New page: 200px<br /><applet load="1mai" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mai, resolution 1.90Å" /> '''STRUCTURE OF THE PLE...)
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Revision as of 19:09, 20 November 2007
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STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE
Overview
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.
About this Structure
1MAI is a Single protein structure of sequence from Rattus norvegicus with I3P as ligand. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 Full crystallographic information is available from OCA.
Reference
Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain., Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB, Cell. 1995 Dec 15;83(6):1037-46. PMID:8521504
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