The role of exon 5 in fibroblast collagenase (MMP-1) substrate specificity and inhibitor selectivity

European Journal of Biochemistry

Volumn 268, Issue 6, 2001, Pages 1888-1896

  Knäuper, Vera ^a,d   Patterson, Margaret L ^a   Gomis Rüth, Franz X ^b   Smith, Bryan ^c   Lyons, Alan ^c   Docherty, Andrew J P ^c   Murphy, Gillian ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

^c UCB PHARMA   (Belgium)

^d UNIVERSITY OF YORK   (United Kingdom)

Author keywords

Collagenolysis; Inhibitor; MMP 1; MMP 3; TIMP

Indexed keywords

CELL ENZYME; COLLAGEN TYPE 1; COLLAGENASE; GELATIN; INTERSTITIAL COLLAGENASE; ISOENZYME; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TRYPSIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CHIMERA; COLLAGEN DEGRADATION; CONTROLLED STUDY; DNA CLEAVAGE; ENZYME ACTIVITY; ENZYME INHIBITOR COMPLEX; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; EXON; FIBROBLAST; GENE ACTIVITY; GENE CONSTRUCT; GENE FUNCTION; HUMAN; PHENOTYPE; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; EXONS; FIBROBLASTS; KINETICS; MATRIX METALLOPROTEINASE 1; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEASE INHIBITORS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0034830712     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02062.x     Document Type: Article

References (38)

1. Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein
2. Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases
3. Comparison of human stromelysin and collagenase by cloning and sequence analysis
4. Molecular cloning and expression of collagenase-3, a novel human matrix metallopro-teinase produced by breast carcinomas
5. Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage
6. A matrix metalloproteinase expressed on the surface of invasive tumour cells
7. Fragments of human fibroblast collagenase. Purification and characterisation
8. Fragmentation of human polymorphonuclear-leucocyte collagenase
9. Biochemical characterization of human collagenase-3
10. The role of the c-terminal domain of human collagenase-3 (MMP- 13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
11. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
12. Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases
13. The role of the C-terminal domain in collagenase and stromelysin specificity
14. Structure-function relationship of human neutrophil collagenase: Identification of regions responsible for substrate specificity and general proteinase activity
15. Collagen binding site in collagenase can be determined using the concept of sense- antisense peptide interactions
16. Analysis of the contribution of the hinge region of human neutrophil collagenase (HNC, MMP-8) to stability and collagenolytic activity by alanine scanning mutagenesis
17. Role of the zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins
18. Identification of the 183RWTNNFREY191 region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity
19. Crystal structure of the stromelysin catalytic domain at 2.0 Å resolution: Inhibitor-induced conformational changes
20. Site-directed mutagenesis by overlap extension using the polymerase chain reaction
21. r active forms, and a comparison of recombinant with natural stromelysin activities
22. The activation of latent pig synovial collagenase
23. A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases
24. The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: A kinetic analysis of the inhibition of gelatinase A
25. Metho-trexate, a high-affinity pseudosubstrate of dihydrofolate reductase
26. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
27. 1.56 A structure of mature truncated human fibroblast collagenase
28. Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
29. Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor
30. Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor
31. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller
32. The NMR structure of the inhibited catalytic domain of human stromelysin-1
33. X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design
34. Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes
35. Sequence specificities of human fibroblast and neutrophil collagenases
36. Analysis of the interaction of TIMP-2 and MMPs: Engineering the changes
37. The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity
38. Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluorometric assays