2TN4
FOUR CALCIUM TNC
Summary for 2TN4
| Entry DOI | 10.2210/pdb2tn4/pdb |
| Descriptor | TROPONIN C, CALCIUM ION (3 entities in total) |
| Functional Keywords | contractile system protein, calcium regulation, calmodulin superfamily |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 18272.35 |
| Authors | Love, M.L.,Dominguez, R.,Houdusse, A.,Cohen, C. (deposition date: 1997-09-18, release date: 1998-04-08, Last modification date: 2024-05-22) |
| Primary citation | Houdusse, A.,Love, M.L.,Dominguez, R.,Grabarek, Z.,Cohen, C. Structures of four Ca2+-bound troponin C at 2.0 A resolution: further insights into the Ca2+-switch in the calmodulin superfamily. Structure, 5:1695-1711, 1997 Cited by PubMed Abstract: In contrast to Ca2+4-bound calmodulin (CaM), which has evolved to bind to many target sequences and thus regulate the function of a variety of enzymes, troponin C (TnC) is a bistable switch which controls contraction in striated muscles. The specific target of TnC is troponin I (TnI), the inhibitory subunit of the troponin complex on the thin filaments of muscle. To date, only the crystal structure of Ca2+2-bound TnC (i.e. in the 'off' state) had been determined, which together with the structure of Ca2+4-bound CaM formed the basis for the so-called 'HMJ' model of the conformational changes in TnC upon Ca2+ binding. NMR spectroscopic studies of Ca2+4-bound TnC (i.e. in the 'on' state) have recently been carried out, but the detailed conformational changes that take place upon switching from the off to the on state have not yet been described. PubMed: 9438870DOI: 10.1016/S0969-2126(97)00315-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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