The human mast cell tryptase tetramer: a fascinating riddle solved by structure.
Tryptases, the predominant proteins of human mast cells, have been implicated as pathogenetic mediators of allergic and inflammatory conditions, most notably asthma. Until recently, the fascinating properties that distinguish tryptases among the serine proteinases, particularly their activity as a heparin-stabilized tetramer, resistance to most proteinaceous inhibitors, and preference for peptidergic over macromolecular substrates presented a riddle. This review solves this riddle with the help of the crystal structure of the human beta(2)-tryptase tetramer, but also indicates controversies between the unique quaternary architecture and some experimental data.
Sommerhoff
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Abteilung für Klinische Chemie und Klinische Biochemie in der Chirurgischen Klinik Innenstadt, Klinikum der Ludwig-Maximilians-Universität, Nussbaumstrasse 20, D-80336, Munich, Germany. sommerhoff@clinbio.med.uni-muenchen.de
Bode
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Matschiner
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Bergner
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Fritz
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D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D053818:Chymases; D004795:Enzyme Stability; D006801:Humans; D008407:Mast Cells / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry; D013379:Substrate Specificity; D053802:Tryptases
D011506:Proteins; D015842:Serine Proteinase Inhibitors; C090901:leech-derived tryptase inhibitor C; D012697:Serine Endopeptidases; C083294:chymase 2; D053818:Chymases; D053802:Tryptases