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Structural similarity between the pleckstrin homology domain and verotoxin: The problem of measuring and evaluating structural similarity
Author(s) -
Orengo C.A.,
Swindells M.B.,
Michie A.D.,
Zvelebil M.J.,
Driscoll P.C.,
Waterfield M.D.,
Thornton J.M.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041003
Subject(s) - pleckstrin homology domain , structural similarity , similarity (geometry) , homology (biology) , computational biology , homology modeling , domain (mathematical analysis) , sequence homology , chemistry , biology , biochemistry , computer science , peptide sequence , mathematics , enzyme , artificial intelligence , amino acid , gene , signal transduction , mathematical analysis , image (mathematics)
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.