Definition of an Interface Implicated in Gelsolin Binding to the Sides of Actin Filaments
| Autor: | J. Feinberg, C. Roustan, Y. Benyamin |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Binding Sites
biology Chemistry Biophysics Arp2/3 complex Actin remodeling macromolecular substances Cell Biology In Vitro Techniques Microfilament Filamin Biochemistry Actins Peptide Fragments Cell biology biology.protein Animals Rabbits Actin-binding protein MDia1 Molecular Biology Gelsolin Actin Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 209:426-432 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1995.1520 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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