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Identification of a new cryptic lipid‐binding domain in Ecm25.

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Presentation on theme: "Identification of a new cryptic lipid‐binding domain in Ecm25."— Presentation transcript:

1 Identification of a new cryptic lipid‐binding domain in Ecm25.
Identification of a new cryptic lipid‐binding domain in Ecm25. (A) Structure‐based alignment of Ecm25 and five known CRAL/TRIO domain. Conserved hydrophobic sites are colored blue, polar sites are red, invariant residues are boxed, sites occupied by small residues are magenta and the ligand‐binding sites of the structures are colored gray. Secondary structure elements are numbered according to the canonical C‐terminal CRAL/TRIO domain structure of Sec14 (PDB:1aua), and grayed out when disrupted or absent in some of the structures. Sequences prefixed with ‘h’ are from human; all others are from S. cerevisiae. (B) The truncated Ecm25‐CRAL/TRIO binds to artificial membranes in flotation assays. Liposomes contain 1 mM 1‐palmitoyl‐2‐oleoyl‐snglycero‐3‐phosphocholine (POPC) and phosphatidylserine (PS), PtdIns or PtdIns(3,4,5)P3, as indicated (3%, molar). Ecm25‐CRAL/TRIO was analyzed by western blot. Oriol Gallego et al. Mol Syst Biol 2010;6:430 © as stated in the article, figure or figure legend


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