Solution structure of bovine angiogenin by 1H nuclear magnetic resonance spectroscopy.
The three-dimensional structure of bovine angiogenin has been determined using two- and three-dimensional proton NMR spectroscopy. The solution structure is very close to that recently determined by X-ray diffraction analysis. This structure appears well defined, even if five loops and one helix exhibit greater flexibility. Analysis of the active site geometry confirms the position of the Glu-118 residue which obstructs the pyrimidine binding site. There is no experimental evidence of an unobstructed conformation of angiogenin in solution. In addition, it appears that the Glu-118 and Ser-119 residues and the cell receptor binding loop may play an important role in the differences of C-terminal fragment organization and ribonucleolytic activity observed between angiogenins and ribonuclease A.
Lequin
O
O
Départment de Chimie-Synthèse Organique, URA 1308 du CNRS, Ecole Polytechnique, Palaiseau, France.
Albaret
C
C
Bontems
F
F
Spik
G
G
Lallemand
J Y
JY
D043925:Angiogenesis Inducing Agents / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D012996:Solutions
D043925:Angiogenesis Inducing Agents; D011506:Proteins; D012996:Solutions; C046366:angiogenin; D012259:Ribonuclease, Pancreatic