NMR structure of a Phosphatidyl-ethanolamine Binding Protein from drosophila

Gilles J. P. Rautureau (1) , Françoise Vovelle (2) , Françoise Schoentgen (3) , Martine Decoville (2) , Daniel Locker (2) , Christian Damblon (4) , Laurence Jouvensal (2)

1 WEHI - The Walter and Eliza Hall Institute of Medical Research
2 CBM - Centre de biophysique moléculaire
3 IMPMC - Institut de minéralogie et de physique des milieux condensés
4 Chimie Biologique Structurale, Institut de Chimie, Sart-Tilman (B6c)

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

Mots clés: PEBP; RKIP; phosphatidylethanolamine binding protein; raf kinase inhibitor protein

Domaines: Biochimie, Biologie Moléculaire

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, 2010, 78 (6), pp.1606-1610. ⟨10.1002/prot.22682⟩. ⟨hal-00453409⟩