6HCI

Crystal structure of titin M3 domain

Summary for 6HCI

• Entry DOI: 10.2210/pdb6hci/pdb
• Descriptor: Titin, SULFATE ION (3 entities in total)
• Functional Keywords: titin, ig domains, sarcomere, m-band, transferase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 47861.54

Authors

Chatziefthimiou, S.D.,Ugurlar, D.,Wilmanns, M. (deposition date: 2018-08-15, release date: 2019-08-28, Last modification date: 2024-05-01)

Primary citation

Chatziefthimiou, S.D.,Hornburg, P.,Sauer, F.,Mueller, S.,Ugurlar, D.,Xu, E.R.,Wilmanns, M.
Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment.
Plos One, 14:e0226693-e0226693, 2019

PubMed 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.

PubMed: 31856237
DOI: 10.1371/journal.pone.0226693

Experimental method

X-RAY DIFFRACTION (2.12 Å)