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==Solution structure of fly troponin C, isoform F1== | |||
<StructureSection load='2jnf' size='340' side='right'caption='[[2jnf]]' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lethocerus_indicus Lethocerus indicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JNF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jnf OCA], [https://pdbe.org/2jnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jnf RCSB], [https://www.ebi.ac.uk/pdbsum/2jnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jnf ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q868D4_9HEMI Q868D4_9HEMI] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jn/2jnf_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jnf ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:17637342</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jnf" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Troponin 3D structures|Troponin 3D structures]] | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lethocerus indicus]] | [[Category: Lethocerus indicus]] | ||
[[Category: Bullard B]] | |||
[[Category: Bullard | [[Category: De Nicola GF]] | ||
[[Category: Nicola | [[Category: Pastore A]] | ||
[[Category: Pastore | |||
Latest revision as of 13:08, 20 December 2023
Solution structure of fly troponin C, isoform F1Solution structure of fly troponin C, isoform F1
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTo 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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