Three-dimensional, sequence order-independent structural comparison of a serine protease against the crystallographic database reveals active site similarities: potential implications to evolution and to protein folding.

@article{Fischer1994ThreedimensionalSO,
  title={Three-dimensional, sequence order-independent structural comparison of a serine protease against the crystallographic database reveals active site similarities: potential implications to evolution and to protein folding.},
  author={Daniel Fischer and Hannah Wolfson and Shoei Loong Lin and Ruth Nussinov},
  journal={Protein science : a publication of the Protein Society},
  year={1994},
  volume={3 5},
  pages={
          769-78
        }
}
We have recently developed a fast approach to comparisons of 3-dimensional structures. Our method is unique, treating protein structures as collections of unconnected points (atoms) in space. It is completely independent of the amino acid sequence order. It is unconstrained by insertions, deletions, and chain directionality. It matches single, isolated amino acids between 2 different structures strictly by their spatial positioning regardless of their relative sequential position in the amino… CONTINUE READING
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