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From the first to the second domain of gelsolin: a common path on the surface of actin?
- Source :
-
FEBS letters [FEBS Lett] 2003 Sep 25; Vol. 552 (2-3), pp. 86-90. - Publication Year :
- 2003
-
Abstract
- We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.
- Subjects :
- Animals
Binding Sites
Crystallography, X-Ray
Humans
In Vitro Techniques
Macromolecular Substances
Models, Molecular
Peptide Fragments chemistry
Peptide Fragments metabolism
Protein Structure, Tertiary
Rabbits
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Actins metabolism
Gelsolin chemistry
Gelsolin metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 552
- Issue :
- 2-3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 14527665
- Full Text :
- https://doi.org/10.1016/s0014-5793(03)00934-7