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The phalloidin binding site of F‐actin.
Author(s) -
Vandekerckhove J.,
Deboben A.,
Nassal M.,
Wieland T.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb04008.x
Subject(s) - phalloidin , biology , methionine , binding site , actin , amino acid , biochemistry , microbiology and biotechnology , stereochemistry , chemistry , cytoskeleton , cell
Tritium‐containing affinity‐labelling derivatives of phalloidin, an alkylating iodoacetyl compound (EAL) and a photolabile, carbene generating diazirine (PAL), have been reacted with rabbit muscle actin, the former after protection of thiol groups with N‐ethylmaleimide. Labelled peptides generated by tryptic and/or thermolysin digestion were isolated by paper peptide mapping and characterized by determination of their amino acid sequences. EAL binds to methionine‐119 and methionine‐355; PAL binds to glutamic acid‐117. These residues are located in regions with extremely conserved amino acid sequences. The cleft between the two domains of the actin monomer is suggested as the possible binding site for phalloidin.