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. 2002 Nov;83(5):2716–2725. doi: 10.1016/S0006-3495(02)75281-8

Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping.

Inna Krieger 1, Alla Kostyukova 1, Atsuko Yamashita 1, Yasushi Nitanai 1, Yuichiro Maéda 1
PMCID: PMC1302356  PMID: 12414704

Abstract

Tropomodulin is the unique pointed-end capping protein of the actin-tropomyosin filament. By blocking elongation and depolymerization, tropomodulin regulates the architecture and the dynamics of the filament. Here we report the crystal structure at 1.45-A resolution of the C-terminal half of tropomodulin (C20), the actin-binding moiety of tropomodulin. C20 is a leucine-rich repeat domain, and this is the first actin-associated protein with a leucine-rich repeat. Binding assays suggested that C20 also interacts with the N-terminal fragment, M1-M2-M3, of nebulin. Based on the crystal structure, we propose a model for C20 docking to the actin subunit at the pointed end. Although speculative, the model is consistent with the idea that a tropomodulin molecule competes with an actin subunit for a pointed end. The model also suggests that interactions with tropomyosin, actin, and nebulin are all possible sources of influences on the dynamic properties of pointed-end capping by tropomodulin.

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Selected References

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