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- Title
Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod.
- Authors
McCoy, A J; Fucini, P; Noegel, A A; Stewart, M
- Abstract
Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. The extended molecule has an N-terminal 250-residue actin-binding domain and a rod constructed from six 100-residue repeats that have an Ig fold. The ability to dimerize is crucial to the actin cross-linking function of gelation factor and is mediated by the rod in which the two chains are arranged in an antiparallel fashion. We report the 2.2 A resolution crystal structure of rod domains 5 and 6, which shows that dimerization is mediated primarily by rod domain 6 and is the result of a double edge-to-edge extension of beta-sheets. Thus, contrary to earlier proposals, the chains of the dimeric gelation factor molecule overlap only within domain 6, and domains 1-5 do not pair with domains from the other chain. This information allows construction of a model of the gelation factor molecule and suggests how the chains in the related molecule filamin (ABP280) may interact.
- Publication
Nature structural biology, 1999, Vol 6, Issue 9, p836
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/12296