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A Preliminary Three-Dimensional Structure of Angiogenin
K. A. Palmer, H. A. Scheraga, J. F. Riordan and B. L. Vallee
Proceedings of the National Academy of Sciences of the United States of America
Vol. 83, No. 7 (Apr. 1, 1986), pp. 1965-1969
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/27118
Page Count: 5
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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.
Proceedings of the National Academy of Sciences of the United States of America © 1986 National Academy of Sciences