The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20
MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
Mad2; spindle checkpoint protein Mad2; MAD2-LIKE 1; HSMAD2; mitotic feedback control protein Madp2
GSITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVI SNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWE ESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND
the solution structure of the free Mad2 protein
This sequence is identified using phage display
The structure was determined using triple-resonance NMR spectroscopy
The structures are based on a total of 3124 restraints, 2535 are NOE-derived distance constraints, 363 dihedral angle restraints,226 distance restraints from hydrogen bonds.
0.8mM Mad2 protein U-15N; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
0.8mM Mad2 protein U-15N, 13C, 2H; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
0.8mM Mad2 protein U-15N, 13C; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
0.8mM Mad2 protein U-15N, 13C, U-60% 2H; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
0.8mM MBP1 U-15N; 1mM Mad2 protein NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
0.8mM MBP1 U-15N, 13C; 1mM Mad2 protein NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
protein-peptide complex, MAD2 FAMILY, CELL CYCLE
QGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVI SNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWE ESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND