1YA5

Crystal structure of the titin domains z1z2 in complex with telethonin

1YA5 の概要

• エントリーDOI: 10.2210/pdb1ya5/pdb
• 分子名称: N2B-TITIN ISOFORM, TELETHONIN, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: telethonin; t-cap; ig-like domains; z1; z2; titin, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, myofibril, sarcomere: O15273
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54266.00

構造登録者

Pinotsis, N.,Popov, A.,Zou, P.,Wilmanns, M. (登録日: 2004-12-17, 公開日: 2005-12-20, 最終更新日: 2024-02-14)

主引用文献

Zou, P.,Pinotsis, N.,Lange, S.,Song, Y.H.,Popov, A.,Mavridis, I.,Mayans, O.M.,Gautel, M.,Wilmanns, M.
Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk
Nature, 439:229-233, 2006

PubMed Abstract: 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.

PubMed: 16407954
DOI: 10.1038/nature04343

実験手法

X-RAY DIFFRACTION (2.445 Å)