STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS
Structural basis for phosphoserine-proline recognition by group IV WW domains.
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1
GSHGMADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQE KITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGI HIILRTE
100 mM MOPSO-Na+, 28% PEG 8000, 2 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
1PIN contains the same protein but not complexed
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1 (E.C. 5.2.1.8)
The biological assembly is a monomer of Pin1 bound to the phosphorylated peptide
Peptidyl-Proline Isomerase, WW domain, phosphoserine binding, ISOMERASE
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITR TKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIIL RTE