P. R. Mittl

Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes.

Mittl, P. R., Schulz, G. E.

The crystal structure of the dimeric flavoenzyme glutathione reductase from Escherichia coli was determined and refined to an R-factor of 16.8% at 1.86 A resolution. The molecular 2-fold axis of the...

Anatomy of an engineered NAD-binding site.

Mittl, P. R., Berry, A., Scrutton, N. S., Perham, R. N., Schulz, G. E.

The coenzyme specificity of Escherichia coli glutathione reductase was switched from NADP to NAD by modifying the environment of the 2'-phosphate binding site through a set of point mutations: A179G,...

The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding.

Mittl, P. R., Priestle, J. P., Cox, D. A., McMaster, G., Cerletti, N., Grütter, M. G.

Transforming growth factors beta belong to a group of cytokines that control cellular proliferation and differentiation. Five isoforms are known that share approximately 75% sequence identity, but...