CHARACTERIZATION OF TARGETING DOMAINS BY SEQUENCE-ANALYSIS - GLYCOGEN-BINDING DOMAINS IN PROTEIN PHOSPHATASES

The prediction of functional features from sequence data can powerfull y complement experimental analyses. Domains are delineated in a first step. Subsequent analysis can provide functional information that even may include precise structural details. This contribution describes t he way in which sequence analysis has used multiple alignment, blast a nd reverse blast searches, and other, more sophisticated techniques to produce a detailed picture of the glycogen-targeting domain in the gl ycogen-binding subunit of the protein phosphatase 1 (PP1) family that includes its three-dimensional fold.