Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: A new frontier in timp engineering

Protein Science

Volumn 11, Issue 10, 2002, Pages 2493-2503

  Lee, Meng Huee ^a   Maskos, Klaus ^b   Knäuper, Vera ^c   Dodds, Philippa ^a   Murphy, Gillian ^a,c  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Binding affinity; Functional epitopes; N TIMP 1 as scaffold; N TIMP 3; TACE interactions

Indexed keywords

ARGININE; EPITOPE; ISOENZYME; LEUCINE; SERINE PROTEINASE; SOLVENT; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

AMINO ACID METABOLISM; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME ENGINEERING; ENZYME INHIBITION; ENZYME MODIFICATION; ENZYME STRUCTURE; EPITOPE MAPPING; HYPOTHESIS; MODEL; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN VARIANT;

ADAM PROTEINS; AMINO ACID SEQUENCE; EPITOPE MAPPING; EPITOPES; HUMANS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT; TISSUE INHIBITOR OF METALLOPROTEINASE-1; TISSUE INHIBITOR OF METALLOPROTEINASE-3;

MAMMALIA;

EID: 0036786494     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0216202     Document Type: Article

References (21)

1. Adenovirus-mediated gene delivery of tissue inhibitor of metalloproteinases-3 inhibits invasion and induces apoptosis in melanoma cells
2. TNF-α converting enzyme (TACE) is inhibited by TIMP-3
3. A metalloproteinase disintegrin that releases tumor-necrosis factor-α from cells
4. Localization of the death domain of tissue inhibitor of metalloproteinase-3 to the N-terminus
5. Tissue inhibitor of metalloproteinase-3 induces a Fas-associated death domain-dependent type II apoptotic pathway
6. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
7. Folding and characterization of the amino-terminal domain of human tissue inhibitor of Metalloproteinases-1 (TIMP-1) expressed at high yield in E. coli
8. TIMP-3 Is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5)
9. Full-length and N-TIMP-3 display equal inhibitory activities towards TNF-α convertase
10. The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3
11. Engineering N-terminal domain of TIMP-3 to be a better inhibitor against tumor necrosis factor-α converting enzyme
12. The immuno-inflammatory reaction in Crohn's disease and ulcerative colitis: Characterization, genetics and clinical application. Focus on TNF-α
13. Crystal structure of the catalytic domain of human tumour necrosis factor-α-converting enzyme
14. Specific sequence elements are required for the expression of functional tumor necrosis factor α-converting enzyme (TACE)
15. The behavior and significance of slow binding enzyme inhibitors
16. High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3
17. Tumour necrosis factor-α (TNF-α) converting enzyme contributes to production of TNF-α in synovial tissues from patients with rheumatoid arthritis
18. Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 Å resolution
19. Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family
20. NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit recognition of matrix metalloproteinases
21. TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix