Journal Article

PUBDB-2024-00932

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment

Chatziefthimiou, S. D. ; Hornburg, P. ; Sauer, F. ; Mueller, S. ; Ugurlar, D. ; Xu, E.-R. ; Wilmanns, M. (Corresponding author)Extern*EMBL*

2019
PLOS San Francisco, California, US

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Please use a persistent id in citations: doi:10.1371/journal.pone.0226693  doi:10.3204/PUBDB-2024-00932

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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Contributing Institute(s):

1. EMBL (EMBL)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. DORIS Beamline K1.3 (DORIS III)
2. DORIS Beamline K1.2 (DORIS III)

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