NMR structure of a Phosphatidyl-ethanolamine Binding Protein from drosophila

Abstract : CG7054 is a 179-residue protein from Drosophila melanogaster that has been shown from sequence analysis to be a member of the ‘Phosphatidyl-Ethanolamine-Binding Protein' (PEBP) family1 [Pfam PF01161]. This family containing more than 500 proteins is widely distributed from bacteria to mammals. In mammals, bovine PEBP (bPEBP) was initially characterized as a phospholipid binding protein2, but has also been shown to bind nucleotides and opioids3. The most abundant isoform in human, PEBP-1 (hPEBP-1/RKIP), has been described to modulate important cell mechanisms such as the control of heterotrimeric G-proteins4, the inhibition of mitogen-actived protein-kinase5, nuclear factor-kappa B signaling pathways6 and of serine proteases thrombin, neuropsin and chymotrypsin7. Human PEBP-1 is implicated in metastasis formation8 and Alzheimer's disease
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Submitted on : Thursday, February 4, 2010 - 3:35:02 PM
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Gilles J. P. Rautureau, Françoise Vovelle, Françoise Schoentgen, Martine Decoville, Daniel Locker, et al.. NMR structure of a Phosphatidyl-ethanolamine Binding Protein from drosophila. Proteins - Structure, Function and Bioinformatics, Wiley, 2010, 78 (6), pp.1606-1610. ⟨10.1002/prot.22682⟩. ⟨hal-00453409⟩



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