title: Computer analyses suggest interactions of non-muscle filamin with lipid membranes.
abstract: It is concluded from structure predictions of the primary amino acid sequence by computer analyses that two segments of non-muscle filamin could facilitate lipid membrane attachment or anchoring. Residues 49-71 of the amino-terminal may attach to phospholipid membranes, and residues 131-155 may anchor in the hydrophobic region of lipid membranes.
authors.affiliation: Technical University of Munich, Garching, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Tempel
authors.forename: W H
authors.initials: WH
authors.lastname: Goldmann
authors.forename: G
authors.initials: G
authors.lastname: Isenberg
mesh_terms: D003285:Contractile Proteins / Q000737:chemistry*; D064448:Filamins; D006801:Humans; D066298:In Vitro Techniques; D008563:Membrane Lipids / Q000737:chemistry*; D008840:Microfilament Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017421:Sequence Analysis; D012995:Solubility; D013329:Structure-Activity Relationship
chemical_list: D003285:Contractile Proteins; D064448:Filamins; D008563:Membrane Lipids; D008840:Microfilament Proteins