1fi5: Difference between revisions
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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=" | [[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 | 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 | 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 | [[Category: Brito, R M.]] | ||
[[Category: Finley, N.]] | [[Category: Finley, N.]] | ||
[[Category: Gaponenko, V.]] | [[Category: Gaponenko, V.]] | ||
[[Category: Gasmi-Seabrook, G | [[Category: Gasmi-Seabrook, G M.]] | ||
[[Category: Howarth, J | [[Category: Howarth, J W.]] | ||
[[Category: Rosevear, P | [[Category: Rosevear, P R.]] | ||
[[Category: Solaro, R | [[Category: Solaro, R J.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
| Line 27: | Line 27: | ||
[[Category: troponin c-troponin i interaction]] | [[Category: troponin c-troponin i interaction]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:53 2008'' | ||