title: Definition of an interface implicated in gelsolin binding to the sides of actin filaments.
abstract: Whereas the interaction of the N-terminal domain of gelsolin with monomeric actin is well known, the location of domains 2-3 interacting with the actin filament during the severing process remains uncertain. In this study we define an interface that supports binding of gelsolin domain 2 along the filament axis. Using specific antibodies and actin peptides, this interface was restricted to two adjacent segments: 1-10 and 18-28 in the N-terminal part of actin sequence.
authors.affiliation: CNRS, UPR 9008 Centre de Recherches de Biochimie Macromol eculaire, INSERM U.249, Université Montpellier I, France.
authors.forename: J
authors.initials: J
authors.lastname: Feinberg
authors.forename: Y
authors.initials: Y
authors.lastname: Benyamin
authors.forename: C
authors.initials: C
authors.lastname: Roustan
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D018260:Gelsolin / Q000378:metabolism*; D066298:In Vitro Techniques; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits
chemical_list: D000199:Actins; D018260:Gelsolin; D010446:Peptide Fragments