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  • Title: Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment.
    Author: Chatziefthimiou SD, Hornburg P, Sauer F, Mueller S, Ugurlar D, Xu ER, Wilmanns M.
    Journal: PLoS One; 2019; 14(12):e0226693. PubMed ID: 31856237.
    Abstract:
    In striated muscles, molecular filaments are largely composed of long protein chains with extensive arrays of identically folded domains, referred to as "beads-on-a-string". It remains a largely unresolved question how these domains have developed a unique molecular profile such that each carries out a distinct function without false-positive readout. This study focuses on the M-band segment of the sarcomeric protein titin, which comprises ten identically folded immunoglobulin domains. Comparative analysis of high-resolution structures of six of these domains ‒ M1, M3, M4, M5, M7, and M10 ‒ reveals considerable structural diversity within three distinct loops and a non-conserved pattern of exposed cysteines. Our data allow to structurally interpreting distinct pathological readouts that result from titinopathy-associated variants. Our findings support general principles that could be used to identify individual structural/functional profiles of hundreds of identically folded protein domains within the sarcomere and other densely crowded cellular environments.
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