Chapter title |
Comparisons of the three-dimensional structures, specificities and glycosylation of renins, yeast proteinase A and cathepsin D.
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Chapter number | 20 |
Book title |
Aspartic Proteinases
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Published in |
Advances in experimental medicine and biology, January 1995
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DOI | 10.1007/978-1-4615-1871-6_20 |
Pubmed ID | |
Book ISBNs |
978-1-4613-5761-2, 978-1-4615-1871-6
|
Authors |
Aguilar, C F, Dhanaraj, V, Guruprasad, K, Dealwis, C, Badasso, M, Cooper, J B, Wood, S P, Blundell, T L, Koelsch, G, Metcalf, P, Vetvicka, V, Fusek, M, Dhanaraj, R R, Pitts, J E, Nugent, P, Orprayoon, P, Uusitalo, J, Penttilä, M, Aguilar, C. F., Dhanaraj, V., Guruprasad, K., Dealwis, C., Badasso, M., Cooper, J. B., Wood, S. P., Blundell, T. L. |
Abstract |
The crystal structures of complexes of the aspartic proteinases, human and mouse renins, yeast proteinase A and cathepsin D, with peptide analogue inhibitors are compared. Differences occur in the relative positions of the domain comprising residues 190-302 (pepsin numbering) compared to the remaining structure and in the nature and position of the irregular regions joining the beta-strands and alpha-helices. The first three of the five residues of the oligosaccharide structures attached to Asn 67 of yeast proteinase and cathepsin D cover the same region of the protein surface. All enzymes have an unusual, proline-rich region (292-297) which acts as a second flap (in addition to that involving residues 72-81). This covers the active site cleft, but can be very close to the substrate/inhibitor at P3' and P4' only in the renins. |
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