$High‐resolution X‐ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme$

High‐resolution X‐ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme

The conformation of the synthetic renin inhibitor CP‐69,799, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been determined by X‐ray diffraction at 1.8 A resolution and refined to the crystallographic R factor of 16%. CP‐69,799 is an oligopeptide transit...

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Veröffentlicht in:	The EMBO journal 1989-08, Vol.8 (8), p.2179-2188
Hauptverfasser:	Sali, A., Veerapandian, B., Cooper, J.B., Foundling, S.I., Hoover, D.J., Blundell, T.L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Aspartic Acid Endopeptidases Binding Sites Biological and medical sciences Chemical Phenomena Chemistry Crystallography Endopeptidases - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Molecular Structure Oligopeptides - metabolism Protease Inhibitors - metabolism Protein Binding Protein Conformation renin X-Ray Diffraction
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