Typical structures and native and cleaved serpins. The structures of native ovalbumin62 and cleaved α1-antitrypsin309 determined by x-ray crystallography
are shown. The α-carbon tracing of the polypeptide backbone is indicated for each protein. The P1 to P12 residues of ovalbumin form an exposed loop on
the surface of the protein that is susceptible to proteolytic attack. After cleavage of the reactive site peptide bond (P1-P1′) of α1-antitrypsin, residues P1 to
P12 become incorporated into a β-sheet structure (thick lines; strands numbered according to α1-antitrypsin), and the P1 and P1′ amino acid residues are
separated by 69Å.
Source: Antithrombin Deficiency, The Online Metabolic and Molecular Bases of Inherited Disease
Citation: Valle D, Beaudet AL, Vogelstein B, Kinzler KW, Antonarakis SE, Ballabio A, Gibson K, Mitchell G. The Online Metabolic and Molecular
Bases of Inherited Disease; 2014 Available at: http://mhmedical.com/ Accessed: July 31, 2017
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