[Structural similarity of regions of activation cleavage of protein-precursors by reactive centers of serpins].
A comparative analysis of primary sequences of the region of "leaving group" of a number of splittings evoked by serine proteinases under the activation of protein-precursors has been carried out. A pronounced domination of amino acids of hydrophobic nature in P2'-position similar to that observed in case of the reactive centres of serpines has been noticed. Physiological role of S2'-stimulation of serine proteinases is discussed.
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D001665:Binding Sites; D006868:Hydrolysis; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011498:Protein Precursors / Q000737:chemistry*; D015843:Serpins / Q000737:chemistry*; D012995:Solubility; D014867:Water / Q000737:chemistry
D000596:Amino Acids; D011498:Protein Precursors; D015843:Serpins; D014867:Water