2jnf: Difference between revisions
New page: left|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== | ||
To gain a molecular description of how muscles can be activated by | 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.]] | ||
[[Category: Nicola, G | [[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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:19 2008'' |
Revision as of 19:04, 21 February 2008
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Solution structure of fly troponin C, isoform F1
OverviewOverview
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 StructureAbout this Structure
2JNF is a Single protein structure of sequence from Lethocerus indicus. Full crystallographic information is available from OCA.
ReferenceReference
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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