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Membrane Metalloendopeptidases in Immune Function and Disease

  • Judith S. Bond
  • Weiping Jiang
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 421)

Abstract

The enzymes that compose the ‘Metallopeptidases’ are a diverse group1. Forty-seven distinct evolutionary families of metallopeptidases have been identified in the last eight years; more than for any other protease classes, i.e., the serine/threonine, cysteine, or aspartic classes of proteases (see the Peptidase World Wide Web sites:http://www.qmw.ac.uk/~ugca000/iupac/enzyme/ and htpp://prolysis.phys.univ-tours.fr/Prolysis). In 1987, the primary amino acid sequence of very few metallopeptidases and of only one mammalian metalloendopeptidase (human fibroblast collagenase) were known, and the 3-dimensional structures of very few metallopeptidases (thermolysin, carboxypeptidase A and B) were solved2. 3. Now hundreds of sequences of members of this Class are known, and many x-ray structures have been determined to high resolution (see, for example, reference 4). Thus our information about this class is expanding rapidly.

Keywords

Major Histocompatibility Complex Myelin Basic Protein Snake Venom Primary Amino Acid Sequence Major Histocompatibility Complex Genotypes42 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Judith S. Bond
    • 1
  • Weiping Jiang
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyThe Pennsylvania State University College of MedicineHersheyUSA

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