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A prediction of the secondary structure of the pleckstrin homology domain
Author(s) -
Jenny Thomas F.,
Benner Steven A.
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340200102
Subject(s) - pleckstrin homology domain , homology (biology) , computational biology , protein secondary structure , domain (mathematical analysis) , homology modeling , protein superfamily , protein domain , sequence homology , genetics , bioinformatics , chemistry , biology , peptide sequence , biochemistry , mathematics , amino acid , gene , mathematical analysis , membrane , enzyme
A consensus prediction for the secondary structure of the pleckstrin homology (PH) domain is presented. The prediction is based on an analysis of patterns of conservation and variation of homologous protein sequences. The structure is predicted to be formed largely from beta strands with a single alpha helix. © 1994 Wiley‐Liss, Inc.