An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases

An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases

Show other versions (1)

The analysis reported here describes detailed structural studies of endothiapepsin (the aspartic proteinase from Endothia parasitica), with and without bound inhibitors, and human pepsin 3b. Comparison of multiple crystal structures of members of the aspartic proteinase family has revealed small but...

Full description

Bibliographic Details
Main Authors: Bailey, D, Carpenter, E, Coker, A, Coker, S, Read, J, Jones, A, Erskine, P, Aguilar, C, Badasso, M, Toldo, L, Rippmann, F, Sanz-Aparicio, J, Albert, A, Blundell, T, Roberts, N, Wood, S, Cooper, J
Format: Journal article
Language:English
Published: 2012

Similar Items

Similar Items