RGD Reference Report - Structure and dynamics of the phospholipase C-delta1 pleckstrin homology domain located at the lipid bilayer surface. - Rat Genome Database

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Structure and dynamics of the phospholipase C-delta1 pleckstrin homology domain located at the lipid bilayer surface.

Authors: Tuzi, S  Uekama, N  Okada, M  Yamaguchi, S  Saito, H  Yagisawa, H 
Citation: Tuzi S, etal., J Biol Chem 2003 Jul 25;278(30):28019-25. Epub 2003 May 7.
RGD ID: 1299011
Pubmed: PMID:12736268   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M300101200   (Journal Full-text)

Despite the importance of signal transduction pathways at membrane surfaces, there have been few means of investigating their molecular mechanisms based on the structural information of membrane-bound proteins. We applied solid state NMR as a novel method to obtain structural information about the phospholipase C-delta1 (PLC-delta1) pleckstrin homology (PH) domain at the lipid bilayer surface. NMR spectra of the alanine residues in the vicinity of the beta5/beta6 loop in the PH domain revealed changes in local conformations due to the membrane localization of the protein. We propose that these conformational changes originate from a hydrophobic interaction between the amphipathic alpha-helix located in the beta5/beta6 loop and the hydrophobic layer of the membrane and contribute to the membrane binding affinity, interdomain interactions and intermolecular interactions of PLC-delta1.

Objects referenced in this article
Gene Plcd1 phospholipase C, delta 1 Rattus norvegicus

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