Binding of gelsolin domain 2 to actin
| Autor: | Celine Renoult, Yves Benyamin, Claude Roustan, Abdellatif Fattoum, Fabrice Raynaud, Laurence Blondin, Sutherland K. Maciver, Diane Ternent |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Protein Folding Macromolecular Substances macromolecular substances In Vitro Techniques Binding Competitive Biochemistry Protein structure Spectroscopy Fourier Transform Infrared Animals Humans Actin-binding protein Gelsolin Actin Binding Sites biology Chemistry Microfilament Proteins Actin remodeling Cofilin Actins Recombinant Proteins Protein Structure Tertiary Cell biology Cross-Linking Reagents Destrin Spectrometry Fluorescence Actin Depolymerizing Factors Actin depolymerizing factor biology.protein Rabbits |
| Zdroj: | European Journal of Biochemistry. 268:6165-6175 |
| ISSN: | 0014-2956 |
| DOI: | 10.1046/j.0014-2956.2001.02574.x |
| Popis: | It is generally assumed that of the six domains that comprise gelsolin, domain 2 is primarily responsible for the initial contact with the actin filament that will ultimately result in the filament being severed. Other actin-binding regions within domains 1 and 4 are involved in gelsolin's severing and subsequent capping activity. The overall fold of all gelsolin repeated domains are similar to the actin depolymerizing factor (ADF)/cofilin family of actin-binding proteins and it has been proposed that there is a similarity in the actin-binding interface. Gelsolin domains 1 and 4 bind G-actin in a similar manner and compete with each other, whereas domain 2 binds F-actin at physiological salt concentrations, and does not compete with domain 1. Here we investigate the domain 2 : actin interface and compare this to our recent studies of the cofilin : actin interface. We conclude that important differences exist between the interfaces of actin with gelsolin domains 1 and 2, and with ADF/cofilin. We present a model for F-actin binding of domain 2 with respect to the F-actin severing and capping activity of the whole gelsolin molecule. |
| Databáze: | OpenAIRE |
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