{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T03:33:52Z","timestamp":1791171232602,"version":"4.1.0"},"reference-count":30,"publisher":"National Academy of Sciences","issue":"31","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2008,8,5]]},"abstract":"<jats:p>The initiation of actin polymerization in cells requires actin filament nucleators. With the exception of formins, known filament nucleators use the Wiskott\u2013Aldrich syndrome protein (WASP) homology 2 (WH2 or W) domain for interaction with actin. A common architecture, found in Spire, Cobl, VopL, and VopF, consists of tandem W domains that tie together three to four actin monomers to form a polymerization nucleus. Uncontrollable polymerization has prevented the structural investigation of such nuclei. We have engineered stable nuclei consisting of an actin dimer and a trimer stabilized by tandem W domain hybrid constructs and studied their structures in solution by x-ray scattering. We show that Spire-like tandem W domains stabilize a polymerization nucleus by lining up actin subunits along the long-pitch helix of the actin filament. Intersubunit contacts in the polymerization nucleus, thought to involve the DNase I-binding loop of actin, coexist with the binding of the W domain in the cleft between actin subdomains 1 and 3. The successful stabilization of filament-like multiactin assemblies opens the way to the crystallographic investigation of intersubunit contacts in the actin filament.<\/jats:p>","DOI":"10.1073\/pnas.0801650105","type":"journal-article","created":{"date-parts":[[2008,7,31]],"date-time":"2008-07-31T21:34:31Z","timestamp":1217540071000},"page":"10785-10790","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":34,"title":["X-ray scattering study of actin polymerization nuclei assembled by tandem W domains"],"prefix":"10.1073","volume":"105","author":[{"given":"Grzegorz","family":"Rebowski","sequence":"first","affiliation":[{"name":"Department of Physiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Malgorzata","family":"Boczkowska","sequence":"additional","affiliation":[{"name":"Department of Physiology, School of Medicine, University of 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