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New page: left|200px<br /><applet load="1fi5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fi5" /> '''NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CA...
 
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[[Image:1fi5.gif|left|200px]]<br /><applet load="1fi5" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fi5.gif|left|200px]]<br /><applet load="1fi5" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fi5" />
caption="1fi5" />
'''NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I.'''<br />
'''NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I.'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1FI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1GGS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FI5 OCA].  
1FI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1GGS. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI5 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Abusamhadneh, E.]]
[[Category: Abusamhadneh, E.]]
[[Category: Brito, R.M.]]
[[Category: Brito, R M.]]
[[Category: Finley, N.]]
[[Category: Finley, N.]]
[[Category: Gaponenko, V.]]
[[Category: Gaponenko, V.]]
[[Category: Gasmi-Seabrook, G.M.]]
[[Category: Gasmi-Seabrook, G M.]]
[[Category: Howarth, J.W.]]
[[Category: Howarth, J W.]]
[[Category: Rosevear, P.R.]]
[[Category: Rosevear, P R.]]
[[Category: Solaro, R.J.]]
[[Category: Solaro, R J.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium binding protein]]
[[Category: calcium binding protein]]
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[[Category: troponin c-troponin i interaction]]
[[Category: troponin c-troponin i interaction]]


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