1WIT
TWITCHIN IMMUNOGLOBULIN SUPERFAMILY DOMAIN (IGSF MODULE) (IG 18'), NMR, MINIMIZED AVERAGE STRUCTURE
Summary for 1WIT
| Entry DOI | 10.2210/pdb1wit/pdb |
| Descriptor | TWITCHIN 18TH IGSF MODULE (1 entity in total) |
| Functional Keywords | immunoglobulin superfamily, i set, muscle protein |
| Biological source | Caenorhabditis elegans |
| Total number of polymer chains | 1 |
| Total formula weight | 10002.41 |
| Authors | Fong, S.,Bycroft, M. (deposition date: 1996-06-23, release date: 1996-12-23, Last modification date: 2024-05-22) |
| Primary citation | Fong, S.,Hamill, S.J.,Proctor, M.,Freund, S.M.,Benian, G.M.,Chothia, C.,Bycroft, M.,Clarke, J. Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J.Mol.Biol., 264:624-639, 1996 Cited by PubMed Abstract: The NMR solution structure of an immunoglobulin superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry-simulated annealing protocol based on 1207 distance and 48 dihedral restraints. The atomic rms distributions about the mean coordinate for the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy atoms. The protein has a topology very similar to that of telokin and the titin Ig domains and thus it falls into the I set of the immunoglobulin superfamily. The close agreement between the predicted and observed structures of Ig 18' demonstrates clearly that the I set profile can be applied in the structure prediction of immunoglobulin-like domains of diverse modular proteins. Folding studies reveal that the protein has relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH. Unfolding studies suggest that the protein has considerable kinetic stability, the half life of the unfolding is greater than 40 minutes in the absence of denaturant. PubMed: 8969309DOI: 10.1006/jmbi.1996.0665 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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