1H, 15N and 13C resonance assignments of CG7054, a new PEBP from Drosophila melanogaster

Abstract

CG7054 is a 179 residue protein from Drosophila melanogaster. Based on sequence alignment, it has been shown that CG7054 belongs to the phosphatidylethanolamine binding proteins (PEBP) family. PEBP proteins are widely distributed in various species, from bacteria to mammals. PEBPs have an affinity for anionic ligands, such as phosphatidylethanolamine, opioids, nucleotides (Bucquoy et al. 1994). Human PEBP-1 is implicated in cancer, acting as a metastase suppressor. During cancer treatment, it sensibilises cells to chemotherapy and immunotherapy. Human PEBP-1 is also implicated in other diseases (Alzheimer's disease, infertility, diabetes...). However, the molecular mechanisms by which PEBPs act remain obscure. These proteins modulate important cell mechanisms involving serine proteases (thrombin, neuropsin and chymotrypsin), G-proteins, MAP-kinase and NFkB signaling pathways. Several crystallographic studies (Serre et al. 1998) have shown that PEBPs share a similar topology, but the solution structure is unknown. In order to gain new insights into structurefunction relationships, dynamics and protein-protein or protein-ligand interactions in solution for this family of proteins, we present herein the assignments (1H, 13C, 15N) of the backbone (complete) and side chain (94%) of CG7054 using conventional triple resonance experiments. The chemical shifts have been deposited in the BioMagResBank under Accession No. 7286.