title: Membrane microstructural templates for enzyme domain formation.
abstract: Soluble proteins can spontaneously self-organize into two-dimensional domains at membrane interfaces, given sufficient mobility and specificity to membrane-localized ligands. The authors' recent results studying interfacial domain formation of the membrane-active enzyme, phospholipase A2, indicate that lateral phase separation of heterogeneous membrane mixtures creates anionic templates of specific morphology onto which the enzyme deposits, forming large protein assemblies. Selective removal of membrane components (lysolipid or fatty acid) produces different enzyme interfacial responses and domain morphologies. This leads to the conclusion that complex chemical and physical interactions laterally in the lipid membrane interface as well as between bound protein molecules play a role in organizing protein structures.
authors.affiliation: Department of Chemistry, Biochemistry and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland, USA.
authors.forename: K M
authors.initials: KM
authors.lastname: Maloney
authors.forename: M
authors.initials: M
authors.lastname: Grandbois
authors.forename: C
authors.initials: C
authors.lastname: Salesse
authors.forename: D W
authors.initials: DW
authors.lastname: Grainger
authors.forename: A
authors.initials: A
authors.lastname: Reichert
mesh_terms: D001665:Binding Sites; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry*; D008566:Membranes; D010741:Phospholipases A / Q000737:chemistry* / Q000378:metabolism; D054467:Phospholipases A2; D010743:Phospholipids; D011485:Protein Binding; D011487:Protein Conformation; D013698:Templates, Genetic
chemical_list: D008055:Lipids; D010743:Phospholipids; D010741:Phospholipases A; D054467:Phospholipases A2