Catalytic domains of matrix metalloproteinases: A molecular biology approach to drug discovery

Qizhuang Ye, Donald Hupe, Linda Johnson

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Molecular biology has provided a range of tools for drug research. The work in the matrix metalloproteinase (MMP) catalytic domain area demonstrated one of the molecular biology approaches to drug discovery. Matrix metalloproteinases are a family of zinc containing proteinases involved in connective tissue remodeling and implicated in diseases such as arthritis, cancer metastasis, and periodontal diseases. Several catalytic domains of human MMPs have been expressed in E. coli and used for random inhibitor screening, protein/inhibitor complex structural determinations, and protein structure-function studies, promising a new generation of MMP inhibitors with high affinity, high selectivity, and high bioavailabitity as therapeutical agents.

Original languageEnglish (US)
Pages (from-to)407-418
Number of pages12
JournalCurrent Medicinal Chemistry
Volume3
Issue number6
StatePublished - 1996
Externally publishedYes

Fingerprint

Molecular biology
Drug Discovery
Matrix Metalloproteinases
Molecular Biology
Catalytic Domain
Matrix Metalloproteinase Inhibitors
Periodontal Diseases
Connective Tissue
Escherichia coli
Arthritis
Zinc
Screening
Proteins
Peptide Hydrolases
Tissue
Neoplasm Metastasis
Research
Pharmaceutical Preparations
Neoplasms

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Organic Chemistry
  • Pharmacology

Cite this

Catalytic domains of matrix metalloproteinases : A molecular biology approach to drug discovery. / Ye, Qizhuang; Hupe, Donald; Johnson, Linda.

In: Current Medicinal Chemistry, Vol. 3, No. 6, 1996, p. 407-418.

Research output: Contribution to journalArticle

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