Crystal structure of human T-cell leukemia virus protease, a novel target for anti-cancer design

Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug design

PVIPLDPARRPVIKAQVDTQTSHPKTIEALLDTGADMTVIPIALFSSNTPLKNTSVLGAGGQTQDHFKLTSLPVLIRLPF
RTTPIVLTSCLVDTKNNWAIIGRDALQQCQGVLYLP

PEG8000, PEG300, DTT and Sodium Acetate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

NCS RESTRAINTS STATISTICS FOR CONFORMATION B OF CHAIN J

NCS RESTRAINTS STATISTICS

NCS GROUP NUMBER : 3
CHAIN NAMES : I J K
NUMBER OF COMPONENTS NCS GROUP : 1
COMPONENT C SSSEQI TO C SSSEQI CODE
1 I 401 I 410 1
1 J 401 J 410 1
1 K 401 K 410 1
GROUP CHAIN COUNT RMS WEIGHT
TIGHT POSITIONAL 3 I (A): 67 ; 0.08 ; 0.05
TIGHT POSITIONAL 3 J (A): 67 ; 0.06 ; 0.05
TIGHT POSITIONAL 3 K (A): 67 ; 0.06 ; 0.05
TIGHT THERMAL 3 I (A**2): 67 ; 0.21 ; 0.50
TIGHT THERMAL 3 J (A**2): 67 ; 0.17 ; 0.50
TIGHT THERMAL 3 K (A**2): 67 ; 0.18 ; 0.50

THE PEPTIDE INHIBITOR WAS SYNTHESIZED ON AN ABI 431 PEPTIDE SYNTHESIZER (0.25 MM SCALE) STARTING WITH H-PRO-2-CHLOROTRITYL RESIN. STANDARD FASTMOC PROTOCOL WAS USED FOR ALL SYNTHETIC CYCLES EXCEPT FOR THE FMOC-STATINE COUPLING REACTION, WHICH WAS CARRIED OUT MANUALLY FOR CA. 14 HR WITH ONLY 2-FOLD MOLAR EXCESS OF FMOC-STATINE. THE COMPLETENESS OF THE COUPLING WAS CONFIRMED BY THE NINHYDRIN TEST. AFTER CLEAVAGE OF THE PEPTIDE FROM THE RESIN, THE CRUDE PRODUCT WAS PURIFIED BY SEMIPREPARATIVE RP-HPLC.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. NCS RESTRAINTS STATISTICS reported in remark 3 corresponds to conformation A of chain J in the coordinates. NCS RESTRAINTS STATISTICS reported in remark 7 corresponds to conformation B of chain J in the coordinates.

PVIPLDPARRPVIKAQVDTQTSHPKTIEALLDTGADMTVLPIALFSSNTPLKNTSVLGAGGQTQDHFKLTSLPVLIRLPF
RTTPIVLTSCLVDTKNNWAIIGRDALQQCQGVLYLP

BINDING SITE FOR CHAIN I OF (ACE)APQV(STA)VMHP PEPTIDE

BINDING SITE FOR CHAIN J OF (ACE)APQV(STA)VMHP PEPTIDE

BINDING SITE FOR CHAIN K OF (ACE)APQV(STA)VMHP PEPTIDE