A prediction of the secondary structure of the pleckstrin homology domain.
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.
Jenny
T F
TF
Department of Chemistry, Swiss Federal Institute of Technology, Zurich.
Benner
S A
SA
D000595:Amino Acid Sequence; D001798:Blood Proteins / Q000737:chemistry*; D003198:Computer Simulation; D017124:Conserved Sequence; D014644:Genetic Variation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010750:Phosphoproteins; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D001798:Blood Proteins; D010750:Phosphoproteins; C039077:platelet protein P47