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Computer analyses suggest interactions of non‐muscle filamin with lipid membranes
Author(s) -
Tempel M.,
Goldmann W.H.,
Isenberg G.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00697-0
Subject(s) - filamin , membrane , phospholipid , chemistry , biochemistry , sequence (biology) , amino acid residue , amino acid , biophysics , peptide sequence , microbiology and biotechnology , biology , cytoskeleton , cell , gene
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.