2jnf

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(New page: 200px<br /><applet load="2jnf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jnf" /> '''Solution structure of fly troponin C, isofor...)
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==Overview==
==Overview==
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To gain a molecular description of how muscles can be activated by, mechanical stretch, we have solved the structure of the calcium-loaded F1, isoform of troponin C (TnC) from Lethocerus and characterized its, interactions with troponin I (TnI). We show that the presence of only one, calcium cation in the fourth EF hand motif is sufficient to induce an open, conformation in the C-terminal lobe of F1 TnC, in contrast with what is, observed in vertebrate muscle. This lobe interacts in a, calcium-independent way both with the N terminus of TnI and, with lower, affinity, with a region of TnI equivalent to the switch and inhibitory, peptides of vertebrate muscles. Using both synthetic peptides and, recombinant proteins, we show that the N lobe of F1 TnC is not engaged in, interactions with TnI, excluding a regulatory role of this domain. These, findings provide insights into mechanically stimulated muscle contraction.
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To gain a molecular description of how muscles can be activated by mechanical stretch, we have solved the structure of the calcium-loaded F1 isoform of troponin C (TnC) from Lethocerus and characterized its interactions with troponin I (TnI). We show that the presence of only one calcium cation in the fourth EF hand motif is sufficient to induce an open conformation in the C-terminal lobe of F1 TnC, in contrast with what is observed in vertebrate muscle. This lobe interacts in a calcium-independent way both with the N terminus of TnI and, with lower affinity, with a region of TnI equivalent to the switch and inhibitory peptides of vertebrate muscles. Using both synthetic peptides and recombinant proteins, we show that the N lobe of F1 TnC is not engaged in interactions with TnI, excluding a regulatory role of this domain. These findings provide insights into mechanically stimulated muscle contraction.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bullard, B.]]
[[Category: Bullard, B.]]
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[[Category: Nicola, G.F.De.]]
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[[Category: Nicola, G F.De.]]
[[Category: Pastore, A.]]
[[Category: Pastore, A.]]
[[Category: ef-hand]]
[[Category: ef-hand]]
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[[Category: troponin c]]
[[Category: troponin c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:16:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:19 2008''

Revision as of 16:04, 21 February 2008


2jnf

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Solution structure of fly troponin C, isoform F1

Overview

To gain a molecular description of how muscles can be activated by mechanical stretch, we have solved the structure of the calcium-loaded F1 isoform of troponin C (TnC) from Lethocerus and characterized its interactions with troponin I (TnI). We show that the presence of only one calcium cation in the fourth EF hand motif is sufficient to induce an open conformation in the C-terminal lobe of F1 TnC, in contrast with what is observed in vertebrate muscle. This lobe interacts in a calcium-independent way both with the N terminus of TnI and, with lower affinity, with a region of TnI equivalent to the switch and inhibitory peptides of vertebrate muscles. Using both synthetic peptides and recombinant proteins, we show that the N lobe of F1 TnC is not engaged in interactions with TnI, excluding a regulatory role of this domain. These findings provide insights into mechanically stimulated muscle contraction.

About this Structure

2JNF is a Single protein structure of sequence from Lethocerus indicus. Full crystallographic information is available from OCA.

Reference

The structure of Lethocerus troponin C: insights into the mechanism of stretch activation in muscles., De Nicola G, Burkart C, Qiu F, Agianian B, Labeit S, Martin S, Bullard B, Pastore A, Structure. 2007 Jul;15(7):813-24. PMID:17637342

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