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Titolo:
Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin
Autore:
Mayans, O; Wuerges, J; Canela, S; Gautel, M; Wilmanns, M;
Indirizzi:
DESY, EMBL Hamburg Outstn, D-22603 Hamburg, Germany DESY Hamburg GermanyD-22603 BL Hamburg Outstn, D-22603 Hamburg, Germany Max Planck Inst Mol Physiol, Dept Phys Biochem, D-44202 Dortmund, Germany Max Planck Inst Mol Physiol Dortmund Germany D-44202 2 Dortmund, Germany
Titolo Testata:
STRUCTURE
fascicolo: 4, volume: 9, anno: 2001,
pagine: 331 - 340
SICI:
0969-2126(20010407)9:4<331:SEFAPR>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN-LIKE MODULES; CALCIUM-RELEASE CHANNEL; I-BAND; SINGLE MOLECULES; DOMAINS; SUPERFAMILY; EXTENSIBILITY; ACTIVATION; STABILITY; EVOLUTION;
Keywords:
immunoglobulin domain; disulphide bridge; I band; titin; muscle elasticity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Wilmanns, M DESY, EMBL Hamburg Outstn, Notkestr 85, D-22603 Hamburg, Germany DESY Notkestr 85 Hamburg Germany D-22603 603 Hamburg, Germany
Citazione:
O. Mayans et al., "Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin", STRUCTURE, 9(4), 2001, pp. 331-340

Abstract

Background: The giant muscle protein titin contributes to the filament system in skeletal and cardiac muscle cells by connecting the Z disk and the central M line of the sarcomere. One of the physiological functions of titinis to act as a passive spring in the sarcomere, which is achieved by the elastic properties of its central I band region. Titin contains about 300 domains of which more than half are folded as immunoglobulin-like (Ig) domains. Ig domain segments of the I band of titin have been extensively used as templates to investigate the molecular basis of protein elasticity. Results: The structure of the Ig domain II from the I band of titin has been determined to 2.1 Angstrom resolution. It reveals a novel, reversible disulphide bridge, which is neither required for correct folding nor changes the chemical stability of ii, but it is predicted to contribute mechanically to the elastic properties of titin in active sarcomeres. From the 92 Ig domains in the longest isoform of titin, at least 40 domains have a potential for disulphide bridge formation. Conclusions: We propose a model where the formation of disulphide bridges under oxidative stress conditions could regulate the elasticity of the I band in titin by increasing sarcomeric resistance. In this model, the formation of the disulphide bridge could refrain a possible directed motion of thetwo beta sheets or other mechanically stable entities of the II Ig domain with respect to each other when exposed to mechanical forces.

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Documento generato il 02/12/20 alle ore 17:08:15