Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/10370
DC Field | Value | Language |
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dc.contributor.author | Gasmi-Seabrook, Geneviève M. C. | - |
dc.contributor.author | Howarth, Jack W. | - |
dc.contributor.author | Finley, Natosha | - |
dc.contributor.author | Abusamhadneh, Ekram | - |
dc.contributor.author | Gaponenko, Vadim | - |
dc.contributor.author | Brito, Rui M. M. | - |
dc.contributor.author | Solaro, R. John | - |
dc.contributor.author | Rosevear, Paul R. | - |
dc.date.accessioned | 2009-06-26T07:37:44Z | - |
dc.date.available | 2009-06-26T07:37:44Z | - |
dc.date.issued | 1999-06-29 | - |
dc.identifier.citation | Biochemistry. 38:26 (1999) 8313-8322 | en_US |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | https://hdl.handle.net/10316/10370 | - |
dc.description.abstract | The N-terminal domain of cardiac troponin I (cTnI) comprising residues 33−80 and lacking the cardiac-specific amino terminus forms a stable binary complex with the C-terminal domain of cardiac troponin C (cTnC) comprising residues 81−161. We have utilized heteronuclear multidimensional NMR to assign the backbone and side-chain resonances of Ca2+-saturated cTnC(81−161) both free and bound to cTnI(33−80). No significant differences were observed between secondary structural elements determined for free and cTnI(33−80)-bound cTnC(81−161). We have determined solution structures of Ca2+-saturated cTnC(81−161) free and bound to cTnI(33−80). While the tertiary structure of cTnC(81−161) is qualitatively similar to that observed free in solution, the binding of cTnI(33−80) results mainly in an opening of the structure and movement of the loop region between helices F and G. Together, these movements provide the binding site for the N-terminal domain of cTnI. The putative binding site for cTnI(33−80) was determined by mapping amide proton and nitrogen chemical shift changes, induced by the binding of cTnI(33−80), onto the C-terminal cTnC structure. The binding interface for cTnI(33−80), as suggested from chemical shift changes, involves predominantly hydrophobic interactions located in the expanded hydrophobic pocket. The largest chemical shift changes were observed in the loop region connecting helices F and G. Inspection of available TnC sequences reveals that these residues are highly conserved, suggesting a common binding motif for the Ca2+/Mg2+-dependent interaction site in the TnC/TnI complex. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | American Chemical Society | en_US |
dc.rights | openAccess | eng |
dc.title | Solution Structures of the C-Terminal Domain of Cardiac Troponin C Free and Bound to the N-Terminal Domain of Cardiac Troponin I | en_US |
dc.type | article | en_US |
dc.identifier.doi | 10.1021/bi9902642 | - |
uc.controloAutoridade | Sim | - |
item.fulltext | Com Texto completo | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.grantfulltext | open | - |
item.languageiso639-1 | en | - |
item.openairetype | article | - |
item.cerifentitytype | Publications | - |
crisitem.author.researchunit | CQC - Coimbra Chemistry Centre | - |
crisitem.author.parentresearchunit | Faculty of Sciences and Technology | - |
crisitem.author.orcid | 0000-0001-9128-2557 | - |
Appears in Collections: | FCTUC Química - Artigos em Revistas Internacionais |
Files in This Item:
File | Description | Size | Format | |
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Solution Structures of the C-Terminal Domain of Cardiac.pdf | 281.21 kB | Adobe PDF | View/Open |
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