Three-dimensional structures of human phospholipase A2 from pancreas and synovial fluid by model building
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Three-dimensional structures of human phospholipase A2 from pancreas and synovial fluid by model building. / Christensen, I T; Jørgensen, Flemming Steen; Svensson, L A; Högberg, T.
In: Drug Design and Discovery, Vol. 10, No. 2, 1993, p. 101-13.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Three-dimensional structures of human phospholipase A2 from pancreas and synovial fluid by model building
AU - Christensen, I T
AU - Jørgensen, Flemming Steen
AU - Svensson, L A
AU - Högberg, T
PY - 1993
Y1 - 1993
N2 - Three-dimensional structures of the enzyme phospholipase A2 (PLA2) from human pancreas and from human synovial fluid were constructed by model building based on high-resolution X-ray crystallographic structures and homology considerations. The structure of the human pancreatic PLA2 was based on the X-ray structure of the highly homologous bovine pancreatic PLA2 (Type I) by amino acid substitution and modification of the C-terminal part followed by geometry relaxation. The structure of the PLA2 from human synovial fluid was constructed from the X-ray structure of PLA2 from Crotalus atrox (Type II) by modification of the calcium binding loop, amino acid substitution, and insertion of two additional amino acid residues followed by geometry relaxation. The structure of the two human PLA2's have been compared and their use as targets for rational design of enzyme inhibitors discussed.
AB - Three-dimensional structures of the enzyme phospholipase A2 (PLA2) from human pancreas and from human synovial fluid were constructed by model building based on high-resolution X-ray crystallographic structures and homology considerations. The structure of the human pancreatic PLA2 was based on the X-ray structure of the highly homologous bovine pancreatic PLA2 (Type I) by amino acid substitution and modification of the C-terminal part followed by geometry relaxation. The structure of the PLA2 from human synovial fluid was constructed from the X-ray structure of PLA2 from Crotalus atrox (Type II) by modification of the calcium binding loop, amino acid substitution, and insertion of two additional amino acid residues followed by geometry relaxation. The structure of the two human PLA2's have been compared and their use as targets for rational design of enzyme inhibitors discussed.
KW - Amino Acid Sequence
KW - Animals
KW - Binding Sites
KW - Calcium
KW - Crotalus
KW - Humans
KW - Models, Molecular
KW - Molecular Sequence Data
KW - Pancreas
KW - Phospholipases A
KW - Phospholipases A2
KW - Protein Conformation
KW - Sequence Alignment
KW - Synovial Fluid
KW - Thermodynamics
M3 - Journal article
C2 - 8399996
VL - 10
SP - 101
EP - 113
JO - Drug Design and Discovery
JF - Drug Design and Discovery
SN - 1055-9612
IS - 2
ER -
ID: 38394440