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Molecular basis of the head‐to‐tail assembly of giant muscle proteins obscurin‐like 1 and titin
Author(s) -
Sauer Florian,
Vahokoski Juha,
Song YoungHwa,
Wilmanns Matthias
Publication year - 2010
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2010.65
Subject(s) - titin , obscurin , sarcomere , immunoglobulin domain , protein filament , heterologous , intermediate filament , biophysics , microbiology and biotechnology , chemistry , biology , biochemistry , antibody , cytoskeleton , myocyte , genetics , cell , gene
Large filament proteins in muscle sarcomeres comprise many immunoglobulin‐like domains that provide a molecular platform for self‐assembly and interactions with heterologous protein partners. We have unravelled the molecular basis for the head‐to‐tail interaction of the carboxyl terminus of titin and the amino‐terminus of obscurin‐like‐1 by X‐ray crystallography. The binary complex is formed by a parallel intermolecular β‐sheet that presents a novel immunoglobulin‐like domain‐mediated assembly mechanism in muscle filament proteins. Complementary binding data show that the assembly is entropy‐driven rather than dominated data by specific polar interactions. The assembly observed leads to a V‐shaped zipper‐like arrangement of the two filament proteins.