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

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...

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Detalhes bibliográficos
Principais autores:	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
Formato:	Journal article
Idioma:	English
Publicado em:	2012

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

Publicado em 2012

Journal article

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

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