STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX WITH THE CDC31P-BINDING DOMAIN FROM KAR1P
Unique Features in the C-terminal Domain Provide Caltractin with Target Specificity
The peptide consists of the cdc31p-binding domain from Kar1p, residues 239-257, and has been chemically synthesized using solid phase F-Moc chemistry. The sequence is naturally found in Saccharomyces cerevisiae (baker's yeast).
structures with the least restraint violations,structures with the lowest energy
the structures are based on a total of 1827 constraints, 1641 are NOE-derived distance constraints, 134 dihedral angle constraints, 52 distance constraints from hydrogen bonds.
1mM CRC-C U-15N,13C; 1.2mM K19 unlabeled.
5mM CaCl2, 25mM Tris, 50mM KCl, 90% H2O, 10% D2O
5mM CaCl2, 25mM Tris, 50mM KCl, 100% D2O
1mM CRC-C unlabeled; 1.2 mM K19 unlabeled.
Guntert, P., Mumenthaler, C. & Wuthrich, K.
Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham III, T.E., DeBolt, S., Ferguson, D., Seibel, G., Kollman, P.
protein-peptide complex, caltractin, KAR1P, calcium-binding, PROTEIN BINDING