The 2.2 å crystal structure of human chymase in complex with succinyl-ala-ala-pro-phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity

This publication has 44 references indexed in Scilit:

• On the size of the active site in proteases. I. Papain
  Published by Elsevier ,2005
• The CCP4 suite: programs for protein crystallography
  Acta Crystallographica Section D-Biological Crystallography, 1994
• SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
  Journal of Molecular Graphics, 1993
• Natural protein proteinase inhibitors and their interaction with proteinases
  European Journal of Biochemistry, 1992
• Crystallographic phasing and refinement of macromolecules: Current Opinion in Structural Biology 1991, 1:1016–1022
  Current Opinion in Structural Biology, 1991
• Substance P regulates the vasodilator activity of calcitonin gene-related peptide
  Nature, 1988
• Bovine chymotrypsinogen A
  Journal of Molecular Biology, 1985
• Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat mast cell proteases, human and dog skin chymases, and human cathepsin G with peptide 4-nitroanilide substrates and with peptide chloromethyl ketone and sulfonyl fluoride inhibitors
  Biochemistry, 1985
• Mast cells at sites of cartilage erosion in the rheumatoid joint.
  Annals of the Rheumatic Diseases, 1984
• The refined crystal structure of bovine β-trypsin at 1·8 Å resolution
  Journal of Molecular Biology, 1975