Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.
The crystal structure of active-site cleaved equine leucocyte elastase inhibitor, a member of the serpin superfamily, has been solved and refined to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite being an intracellular inhibitor with rather low sequence homology of 30% to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the three-dimensional structures are very similar, with deviations only at the sites of insertions and few mobile secondary structure elements. The better resolution in comparison with the structures of other cleaved serpins allows a more precise description of the so-called R-state of the serpins.
Baumann
U
U
Max-Planck-Institut für Biochemie, Martinsried bei München, Germany.
Bode
W
W
Huber
R
R
Travis
J
J
Potempa
J
J
D000595:Amino Acid Sequence; D000818:Animals; D003625:Data Collection / Q000379:methods; D006736:Horses; D006860:Hydrogen Bonding; D007962:Leukocytes / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D015842:Serine Proteinase Inhibitors / Q000737:chemistry*; D015843:Serpins; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
D015842:Serine Proteinase Inhibitors; D015843:Serpins; D014867:Water