Journal of Protein Chemistry

, Volume 16, Issue 4, pp 237–255 | Cite as

Computational Sequence Analysis of the Tissue Inhibitor of Metalloproteinase Family

  • Damon A. Douglas
  • Y. Eric Shi
  • Qingxiang Amy Sang
Article

Abstract

The tissue inhibitor of metalloproteinase (TIMP) family regulates extracellular matrix turnover and tissue remodeling by forming tight-binding inhibitory complexes with matrix metalloproteinases (MMPs). MMPs and TIMPs have been implicated in many normal and pathological processes, such as morphogenesis, development, angiogenesis, and cancer metastasis. This minireview provides information that would aid in classification of the TIMP family and in understanding the similarities and differences among TIMP members according to the physical data, primary structure, and homology values. Calculations of molecular weight, isoelectric point values, and molar extinction coefficients are reported. This study also compares sequence similarities and differences among the TIMP members through calculations of homology within their individual loop regions and the mature region of the molecule. Lastly, this report examines structure–function relationships of TIMPs. Thorough knowledge of TIMP primary and tertiary structure would facilitate the uncovering of the molecular mechanisms underlying metalloproteinase, inhibitory activities and biological functions of TIMPs.

Primary sequence analysis multiple-sequence alignment physical data calculations multi-gap homology calculations structure–function relationship 

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Copyright information

© Plenum Publishing Corporation 1997

Authors and Affiliations

  • Damon A. Douglas
    • 1
  • Y. Eric Shi
    • 2
  • Qingxiang Amy Sang
    • 1
  1. 1.Departments of Chemistry and Institute of Molecular BiophysicsFlorida State UniversityTallahasseeUSA
  2. 2.Departments of Pediatrics and PathologyLong Island Jewish Medical Center, Albert Einstein College of MedicineNew Hyde ParkUSA

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