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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Main Authors: Sali, A, Veerapandian, B, Cooper, J B, Foundling, S I, Hoover, D J, Blundell, T L
Formato: Artigo
Idioma:Inglês
Publicado: 1989
Assuntos:
Research Article
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC401145/
https://ncbi.nlm.nih.gov/pubmed/2676515
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