Determination of the Gelsolin Binding Site on F-actin: Implications for Severing and Capping
Biophysical Journal, ISSN: 0006-3495, Vol: 74, Issue: 2, Page: 764-772
1998
- 57Citations
- 37Captures
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Metrics Details
- Citations57
- Citation Indexes57
- CrossRef57
- 56
- Captures37
- Readers37
- 37
Article Description
Gelsolin is a six-domain protein that regulates actin assembly by severing, capping, and nucleating filaments. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on F-actin. To obtain fully decorated filaments under severing conditions, we have studied a derivative (G2-6) that has a reduced severing efficiency compared to gelsolin. A three-dimensional reconstruction of G2-6:F-actin was obtained by electron cryomicroscopy and helical reconstruction. The structure shows that gelsolin bridges two longitudinally associated monomers when it binds the filament. The F-actin binding region of G2-6 is centered axially at subdomain 3 and radially between subdomains 1 and 3 of the upper actin monomer. Our results suggest that for severing to occur, both gelsolin and actin undergo large conformational changes.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006349598740019; http://dx.doi.org/10.1016/s0006-3495(98)74001-9; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0031879577&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9533689; https://linkinghub.elsevier.com/retrieve/pii/S0006349598740019; http://linkinghub.elsevier.com/retrieve/pii/S0006349598740019; http://api.elsevier.com/content/article/PII:S0006349598740019?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0006349598740019?httpAccept=text/plain
Elsevier BV
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