[HTML][HTML] Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone
PRE Mittl, S Di Marco, JF Krebs, X Bai… - Journal of Biological …, 1997 - ASBMB
The cysteine protease CPP32 has been expressed in a soluble form in Escherichia coli and
purified to> 95% purity. The three-dimensional structure of human CPP32 in complex with
the irreversible tetrapeptide inhibitor acetyl-Asp-Val-Ala-Asp fluoromethyl ketone was
determined by x-ray crystallography at a resolution of 2.3 Å. The asymmetric unit contains a
(p17/p12) 2 tetramer, in agreement with the tetrameric structure of the protein in solution as
determined by dynamic light scattering and size exclusion chromatography. The overall …
purified to> 95% purity. The three-dimensional structure of human CPP32 in complex with
the irreversible tetrapeptide inhibitor acetyl-Asp-Val-Ala-Asp fluoromethyl ketone was
determined by x-ray crystallography at a resolution of 2.3 Å. The asymmetric unit contains a
(p17/p12) 2 tetramer, in agreement with the tetrameric structure of the protein in solution as
determined by dynamic light scattering and size exclusion chromatography. The overall …