 |
PDBsum entry 1mnc
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Hydrolase (metalloprotease)
|
PDB id
|
|
|
|
1mnc
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structure of human neutrophil collagenase reveals large s1' Specificity pocket.
|
 |
|
Authors
|
 |
T.Stams,
J.C.Spurlino,
D.L.Smith,
R.C.Wahl,
T.F.Ho,
M.W.Qoronfleh,
T.M.Banks,
B.Rubin.
|
 |
|
Ref.
|
 |
Nat Struct Biol, 1994,
1,
119-123.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
The crystal structure of the catalytic domain of human neutrophil collagenase
complexed with a peptide transition state analogue has been determined to a
resolution of 2.1 A. The structure of the neutrophil enzyme, when compared with
the three dimensional structure of the corresponding human fibroblast
collagenase, shows differences in the first, S1', of the three enzyme
specificity subsites on the carboxy-terminal side of the substrate scissile
bond. The S1' pocket in the neutrophil collagenase is significantly larger than
the equivalent site in the fibroblast enzyme, suggesting that the former enzyme
has a broader range of possible substrates. Such differences also suggest
approaches for the design of selective matrix metalloproteinase inhibitors.
|
 |
|
|
|
|
 |