| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-86 |
Sentence |
denotes |
Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. |
| T1 |
0-86 |
Sentence |
denotes |
Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. |
| T2 |
87-137 |
Sentence |
denotes |
Implications for structure-based inhibitor design. |
| T2 |
87-137 |
Sentence |
denotes |
Implications for structure-based inhibitor design. |
| T3 |
138-299 |
Sentence |
denotes |
The lysosomal cysteine proteinase cathepsin B (EC 3.4.22.1) plays an important role in protein catabolism and has also been implicated in various disease states. |
| T3 |
138-299 |
Sentence |
denotes |
The lysosomal cysteine proteinase cathepsin B (EC 3.4.22.1) plays an important role in protein catabolism and has also been implicated in various disease states. |
| T4 |
300-395 |
Sentence |
denotes |
The crystal structures of two forms of native recombinant rat cathepsin B have been determined. |
| T4 |
300-395 |
Sentence |
denotes |
The crystal structures of two forms of native recombinant rat cathepsin B have been determined. |
| T5 |
396-498 |
Sentence |
denotes |
The overall folding of rat cathepsin B was shown to be very similar to that of the human liver enzyme. |
| T5 |
396-498 |
Sentence |
denotes |
The overall folding of rat cathepsin B was shown to be very similar to that of the human liver enzyme. |
| T6 |
499-695 |
Sentence |
denotes |
The structure of the native enzyme containing an underivatized active site cysteine (Cys29) showed the active enzyme conformation to be similar to that determined previously for the oxidized form. |
| T6 |
499-695 |
Sentence |
denotes |
The structure of the native enzyme containing an underivatized active site cysteine (Cys29) showed the active enzyme conformation to be similar to that determined previously for the oxidized form. |
| T7 |
696-795 |
Sentence |
denotes |
In a second structure Cys29 was derivatized with the reversible blocking reagent pyridyl disulfide. |
| T7 |
696-795 |
Sentence |
denotes |
In a second structure Cys29 was derivatized with the reversible blocking reagent pyridyl disulfide. |
| T8 |
796-982 |
Sentence |
denotes |
In this structure large side chain conformational changes were observed for the two key catalytic residues Cys29 and His199, demonstrating the potential flexibility of these side chains. |
| T8 |
796-982 |
Sentence |
denotes |
In this structure large side chain conformational changes were observed for the two key catalytic residues Cys29 and His199, demonstrating the potential flexibility of these side chains. |
| T9 |
983-1133 |
Sentence |
denotes |
In addition the structure of the complex between rat cathepsin B and the inhibitor benzyloxycarbonyl-Arg-Ser(O-Bzl) chloromethylketone was determined. |
| T9 |
983-1133 |
Sentence |
denotes |
In addition the structure of the complex between rat cathepsin B and the inhibitor benzyloxycarbonyl-Arg-Ser(O-Bzl) chloromethylketone was determined. |
| T10 |
1134-1246 |
Sentence |
denotes |
The complex structure showed that very little conformational change occurs in the enzyme upon inhibitor binding. |
| T10 |
1134-1246 |
Sentence |
denotes |
The complex structure showed that very little conformational change occurs in the enzyme upon inhibitor binding. |
| T11 |
1247-1329 |
Sentence |
denotes |
It also allowed visualization of the interaction between the enzyme and inhibitor. |
| T11 |
1247-1329 |
Sentence |
denotes |
It also allowed visualization of the interaction between the enzyme and inhibitor. |
| T12 |
1330-1564 |
Sentence |
denotes |
In particular the interaction between Glu245 and the P2 Arg residue was clearly demonstrated, and it was found that the benzyl group of the P1 substrate residue occupies a large hydrophobic pocket thought to represent the S'1 subsite. |
| T12 |
1330-1564 |
Sentence |
denotes |
In particular the interaction between Glu245 and the P2 Arg residue was clearly demonstrated, and it was found that the benzyl group of the P1 substrate residue occupies a large hydrophobic pocket thought to represent the S'1 subsite. |
| T13 |
1565-1655 |
Sentence |
denotes |
This may have important implications for structure-based design of cathepsin B inhibitors. |
| T13 |
1565-1655 |
Sentence |
denotes |
This may have important implications for structure-based design of cathepsin B inhibitors. |