1fi5
From Proteopedia
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|PDB= 1fi5 |SIZE=350|CAPTION= <scene name='initialview01'>1fi5</scene> | |PDB= 1fi5 |SIZE=350|CAPTION= <scene name='initialview01'>1fi5</scene> | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi5 OCA], [http://www.ebi.ac.uk/pdbsum/1fi5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fi5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Rosevear, P R.]] | [[Category: Rosevear, P R.]] | ||
[[Category: Solaro, R J.]] | [[Category: Solaro, R J.]] | ||
- | [[Category: CA]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
[[Category: cardiac]] | [[Category: cardiac]] | ||
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[[Category: troponin c-troponin i interaction]] | [[Category: troponin c-troponin i interaction]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:23:21 2008'' |
Revision as of 17:23, 30 March 2008
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Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I.
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.
About this Structure
1FI5 is a Single protein structure of sequence from Gallus gallus. This structure supersedes the now removed PDB entry 1GGS. Full crystallographic information is available from OCA.
Reference
Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I., Gasmi-Seabrook GM, Howarth JW, Finley N, Abusamhadneh E, Gaponenko V, Brito RM, Solaro RJ, Rosevear PR, Biochemistry. 1999 Jun 29;38(26):8313-22. PMID:10387077
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