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Titolo:
The assembly of immunoglobulin-like modules in titin: Implications for muscle elasticity
Autore:
Improta, S; Krueger, JK; Gautel, M; Atkinson, RA; Lefevre, JF; Moulton, S; Trewhella, J; Pastore, A;
Indirizzi:
European Mol Biol Lab, D-69117 Heidelberg, Germany European Mol Biol Lab Heidelberg Germany D-69117 117 Heidelberg, Germany Chem Sci & Technol Div, Los Alamos, NM USA Chem Sci & Technol Div Los Alamos NM USA Technol Div, Los Alamos, NM USA Univ Rouen, Lab RMN, Mt St Aignan, France Univ Rouen Mt St Aignan France niv Rouen, Lab RMN, Mt St Aignan, France ESBS, UPR 9003, F-67400 Illkirch, France ESBS Illkirch France F-67400ESBS, UPR 9003, F-67400 Illkirch, France
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 3, volume: 284, anno: 1998,
pagine: 761 - 777
SICI:
0022-2836(199812)284:3<761:TAOIMI>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMALL-ANGLE-SCATTERING; 3-DIMENSIONAL NMR-SPECTROSCOPY; MAGNETIC-RESONANCE RELAXATION; MODEL-FREE APPROACH; I-BAND REGION; STRIATED-MUSCLE; SKELETAL-MUSCLE; CRYSTAL-STRUCTURE; LIGHT-SCATTERING; DOMAINS;
Keywords:
connectin; muscle; elasticity; NMR; Ig superfamily;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
79
Recensione:
Indirizzi per estratti:
Indirizzo: Pastore, A European Mol Biol Lab, Meyerhofstr 1, D-69117 Heidelberg, Germany European Mol Biol Lab Meyerhofstr 1 Heidelberg Germany D-69117
Citazione:
S. Improta et al., "The assembly of immunoglobulin-like modules in titin: Implications for muscle elasticity", J MOL BIOL, 284(3), 1998, pp. 761-777

Abstract

Titin, a giant muscle protein, forms filaments that span half of the sarcomere and cover, along their length, quite diversified functions. The regionof titin located in the sarcomere I-band is believed to play a major role in extensibility and passive elasticity of muscle. In the I-band, the titinsequence contains tandem immunoglobulin-like (Ig) modules intercalated by a potentially non-globular region. By a combined approach making use of small angle X-ray scattering and nuclear magnetic resonance techniques, we have addressed the questions of what are the average mutual orientation of poly-Igs and the degree of flexibility around the domain interfaces. Various recombinant fragments containing one, two and four titin I-band tandem domains were analysed. The small-angle scattering data provide a picture of the domains in a mostly extended configuration with their long axes aligned head-to-tail. There is a small degree of bending and twisting of the modules with respect to each other that results in an overall shortening in their maximum linear dimension compared with that expected for the fully extended, linear configurations. This shortening is greatest fur the four module construct (approximate to 15%). N-15 NMR relaxation studies of one and two-domain constructs show that the motions around the interdomain connecting regions are restricted, suggesting that titin behaves as a row of beads connected by rigid hinges. The length of the residues in the interface seems to be the major determinant of the degree of flexibility. Possible implications of our results for the structure and function of titin in muscles are discussed. (C) 1998 Academic Press.

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Documento generato il 04/12/20 alle ore 22:39:26