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001     603747
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024 7 _ |a 10.1371/journal.pone.0226693
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100 1 _ |a Chatziefthimiou, Spyros D.
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245 _ _ |a Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment
260 _ _ |a San Francisco, California, US
|c 2019
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520 _ _ |a 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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700 1 _ |a Hornburg, Philipp
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700 1 _ |a Sauer, Florian
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700 1 _ |a Mueller, Simone
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700 1 _ |a Ugurlar, Deniz
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700 1 _ |a Xu, Emma-Ruoqi
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700 1 _ |a Wilmanns, Matthias
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773 _ _ |a 10.1371/journal.pone.0226693
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856 4 _ |u https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0226693#abstract0
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