BOUND CONFORMATION OF N-TERMINAL CLEAVAGE PRODUCT PEPTIDE MIMIC (P1-P9 OF RELEASE SITE) WHILE BOUND TO HCMV PROTEASE AS DETERMINED BY TRANSFERRED NOESY EXPERIMENTS (P1-P5 SHOWN ONLY), NMR, 32 STRUCTURES
Human cytomegalovirus protease complexes its substrate recognition sequences in an extended peptide conformation.
HCMV PROTEASE R-SITE N-TERMINAL CLEAVAGE PRODUCT
TERESYVKA N-TERMINAL RESIDUES OF R-SITE PEPTIDE
TRANSFERRED NUCLEAR OVERHAUSER EFFECT SPECTROSCOPY 50, 150, 250 MS MIXING TIMES USED TO GENERATE RESTRAINTS
POTENTIAL ENERGY, MINIMAL RESTRAINT VIOLATIONS
REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. CFF95 FORCEFIELD USED.
0.5M NA2SO4, 50MM NACL, 1MM EDTA, 5MM DTT-D10 IN 10% D2O SPIKED WITH TSP-2,2,3,3-D4
SUBSTRIATE CLEAVAGE, BOUND CONFORMATION, EXTENDED CONFORMATION, substrate-based competitive inhibitor design