1quu

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Image:1quu.gif

1quu, resolution 2.5Å

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CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ

Overview

We have determined the crystal structure of the two central repeats in the, alpha-actinin rod at 2.5 A resolution. The repeats are connected by a, helical linker and form a symmetric, antiparallel dimer in which the, repeats are aligned rather than staggered. Using this structure, which, reveals the structural principle that governs the architecture of, alpha-actinin, we have devised a plausible model of the entire, alpha-actinin rod. The electrostatic properties explain how the two, alpha-actinin subunits assemble in an antiparallel fashion, placing the, actin-binding sites at both ends of the rod. This molecular architecture, results in a protein that is able to form cross-links between actin, filaments.

About this Structure

1QUU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments., Djinovic-Carugo K, Young P, Gautel M, Saraste M, Cell. 1999 Aug 20;98(4):537-46. PMID:10481917

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