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Template:STRUCTURE 1ya5

Crystal structure of the titin domains z1z2 in complex with telethonin

Overview

The Z-disk of striated and cardiac muscle sarcomeres is one of the most densely packed cellular structures in eukaryotic cells. It provides the architectural framework for assembling and anchoring the largest known muscle filament systems by an extensive network of protein-protein interactions, requiring an extraordinary level of mechanical stability. Here we show, using X-ray crystallography, how the amino terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the Z-disk ligand telethonin. The pseudosymmetric structure of telethonin mediates a unique palindromic arrangement of two titin filaments, a type of molecular assembly previously found only in protein-DNA complexes. We have confirmed its unique architecture in vivo by protein complementation assays, and in vitro by experiments using fluorescence resonance energy transfer. The model proposed may provide a molecular paradigm of how major sarcomeric filaments are crosslinked, anchored and aligned within complex cytoskeletal networks.

About this Structure

1YA5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk., Zou P, Pinotsis N, Lange S, Song YH, Popov A, Mavridis I, Mayans OM, Gautel M, Wilmanns M, Nature. 2006 Jan 12;439(7073):229-33. PMID:16407954 Page seeded by OCA on Sat May 3 16:03:49 2008