Please use this identifier to cite or link to this item: http://hdl.handle.net/10316/10370
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dc.contributor.authorGasmi-Seabrook, Geneviève M. C.-
dc.contributor.authorHowarth, Jack W.-
dc.contributor.authorFinley, Natosha-
dc.contributor.authorAbusamhadneh, Ekram-
dc.contributor.authorGaponenko, Vadim-
dc.contributor.authorBrito, Rui M. M.-
dc.contributor.authorSolaro, R. John-
dc.contributor.authorRosevear, Paul R.-
dc.date.accessioned2009-06-26T07:37:44Z-
dc.date.available2009-06-26T07:37:44Z-
dc.date.issued1999-06-29-
dc.identifier.citationBiochemistry. 38:26 (1999) 8313-8322en_US
dc.identifier.issn0006-2960-
dc.identifier.urihttp://hdl.handle.net/10316/10370-
dc.description.abstractThe 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.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsopenAccesseng
dc.titleSolution Structures of the C-Terminal Domain of Cardiac Troponin C Free and Bound to the N-Terminal Domain of Cardiac Troponin Ien_US
dc.typearticleen_US
dc.identifier.doi10.1021/bi9902642-
uc.controloAutoridadeSim-
item.fulltextCom Texto completo-
item.grantfulltextopen-
item.languageiso639-1en-
crisitem.author.deptFaculty of Sciences and Technology-
crisitem.author.parentdeptUniversity of Coimbra-
crisitem.author.researchunitCQC - Coimbra Chemistry Centre-
crisitem.author.parentresearchunitFaculty of Sciences and Technology-
crisitem.author.orcid0000-0001-9128-2557-
Appears in Collections:FCTUC Química - Artigos em Revistas Internacionais
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