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- Ludovic R. Otterbein
- Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
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- Philip Graceffa
- Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
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- Roberto Dominguez
- Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
抄録
<jats:p>The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine 5′-triphosphate (ATP) by a mechanism that remains to be elucidated. Actin modified to block polymerization was crystallized in the adenosine 5′-diphosphate (ADP) state, and the structure was solved to 1.54 angstrom resolution. Compared with previous ATP-actin structures from complexes with deoxyribonuclease I, profilin, and gelsolin, monomeric ADP-actin is characterized by a marked conformational change in subdomain 2. The successful crystallization of monomeric actin opens the way to future structure determinations of actin complexes with actin-binding proteins such as myosin.</jats:p>
収録刊行物
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- Science
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Science 293 (5530), 708-711, 2001-07-27
American Association for the Advancement of Science (AAAS)
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キーワード
詳細情報 詳細情報について
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- CRID
- 1361418520601046272
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- NII論文ID
- 80012604430
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- ISSN
- 10959203
- 00368075
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- データソース種別
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- Crossref
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