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. 1995 Apr;68(4 Suppl):12S–18S.

Structural studies on the ribbon-to-helix transition in profilin: actin crystals.

C E Schutt 1, M D Rozycki 1, J K Chik 1, U Lindberg 1
PMCID: PMC1281853  PMID: 7787053

Abstract

Knowledge of the structure of actin in its various conformational states is important for understanding the diverse motile activities carried out by eukaryotic cells. Profilin:actin crystals provide a unique system for studying conformational states of actin, because they exhibit a high degree of polymorphism in response to environmental conditions while maintaining crystalline order. A preliminary comparison of two states of profilin:beta-actin crystals shows that crystal polymorphism involves movements of actin subdomains at hinge points homologous to those found in hexokinase, a protein whose polypeptide fold is related to actin. The homology of the hinge points in actin to those in hexokinase suggests that actin subdomain movements in profilin:beta-actin crystals have functional significance. We discuss how these movements could be related to structural transitions between states of filamentous actin in muscle contraction.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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