1io0
From Proteopedia
|
CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF
Overview
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.
About this Structure
1IO0 is a Single protein structure of sequence from Gallus gallus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping., Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y, Biophys J. 2002 Nov;83(5):2716-25. PMID:12414704
Page seeded by OCA on Sat Nov 24 22:17:00 2007
