Open AccessA preliminary three-dimensional structure of angiogenin.
Author(s) -
Kathleen A. Palmer,
Harold A. Scheraga,
James Riordan,
B L Vallee
Publication year - 1986
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.83.7.1965
Subject(s) - angiogenin , ribonuclease , dihedral angle , pancreatic ribonuclease , bovine pancreatic ribonuclease , energy minimization , s tag , chemistry , protein structure , cleavage (geology) , crystallography , biophysics , biochemistry , biology , genetics , computational chemistry , rna , molecule , hydrogen bond , paleontology , organic chemistry , fracture (geology) , angiogenesis , gene
A preliminary three-dimensional structure of angiogenin has been computed, based on its homology to bovine pancreatic ribonuclease A. A standard-geometry structure of ribonuclease was first obtained from its x-ray coordinates. The fit of the backbone of angiogenin to that of ribonuclease was then optimized by taking account of amino acid deletions and by minimizing its conformational energy-plus-a-penalty distance function constraining its backbone to that of ribonuclease. Side-chain and backbone dihedral angles were allowed to vary throughout the cycles of energy minimization. In the last stages of minimization, the penalty distance function was removed. A low-energy structure resembling ribonuclease was obtained.