Structural similarity between the pleckstrin homology domain and verotoxin: the problem of measuring and evaluating structural similarity

Protein Sci. 1995 Oct;4(10):1977-83. doi: 10.1002/pro.5560041003.

Abstract

An unexpected structural similarity is described between the pleckstrin homology (PH) domain and verotoxin. This similarity has escaped detection primarily due to the differences in topology that exist between the two proteins. By comparing this result with two previously reported similarities for the PH domain, one with the lipocalins and another with the FK506 binding protein, we discuss the problems of measuring and assessing structural similarities.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Bacterial Toxins / chemistry*
  • Binding Sites
  • Blood Proteins / chemistry*
  • Carrier Proteins / chemistry
  • DNA-Binding Proteins / chemistry
  • Enterotoxins / chemistry
  • Heat-Shock Proteins / chemistry
  • Models, Molecular
  • Models, Structural
  • Molecular Sequence Data
  • Phosphoproteins*
  • Protein Conformation*
  • Protein Structure, Secondary*
  • Sequence Homology, Amino Acid
  • Shiga Toxin 1
  • Tacrolimus / metabolism
  • Tacrolimus Binding Proteins

Substances

  • Bacterial Toxins
  • Blood Proteins
  • Carrier Proteins
  • DNA-Binding Proteins
  • Enterotoxins
  • Heat-Shock Proteins
  • Phosphoproteins
  • Shiga Toxin 1
  • platelet protein P47
  • Tacrolimus Binding Proteins
  • Tacrolimus