Post X-Ray Crystallographic Studies of Chymosin Specificity
作者： E. A. Gustchina , P. Majer , L. D. Rumsh , L. M. Ginodman , N. S. Andreeva
DOI: 10.1007/978-1-4615-5373-1_24
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摘要: X-ray crystallographic studies of bovine chymosin (Gilliland et al. 1990; Newman 1991) have shown that the conserved Tyr75 residue (pepsin numbering is used), located in so-called ‘flap’, takes up an unusual position molecules this enzyme. In almost all native aspartic proteinase structures and their complexes with inhibitors, it forms wall S1 binding pocket, hydroxyl group bound to Ser35 through a water molecule, which also highly conserved. contrast, tip flap orthorhombic crystals has conformation, phenolic ring embedded partly S3 pocket (Fig. 1).
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