Evidence for Functional Homology in the F-Actin Binding Domains of Gelsolin and α-Actinin: Implications for the Requirements of Severing and Capping

The F-actin binding domains of gelsolin and α-actinin compete for the same site on actin filaments with similar binding affinities. Both contain tandem repeats of ∼125 amino acids, the first of which is shown to contain the actin-binding site. We have replaced the F-actin binding domain in the NH2-t...

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Bibliographic Details
Published in:	The Journal of cell biology Vol. 119; no. 4; pp. 835 - 842
Main Authors:	Way, M., Pope, B., Weeds, A. G.
Format:	Journal Article
Language:	English
Published:	New York, NY Rockefeller University Press 01-11-1992 The Rockefeller University Press
Subjects:	Actinin - chemistry Actinin - metabolism Actins Actins - metabolism Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Calcium Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - metabolism Contractile proteins Depolymerization Fluorescence Fundamental and applied biological sciences. Psychology Gelsolin Holoproteins Microfilament Proteins - chemistry Microfilament Proteins - metabolism Microfilaments Molecular Sequence Data Monomers Polymerization Proteins Viscosity Actins Microfilament Binding protein Homology Capping Binding site
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