The Greek key is a very common structural motif in proteins. It has be
en traditionally defined as four beta-strands with '+3,-1,-1' topology
. This definition encompasses motifs with several different three-dime
nsional structures. We have classified Greek keys, based on their hydr
ogen bonding patterns, into three groups with similar three-dimensiona
l structures. All examples of Greek keys in each of these classes have
been automatically extracted using a set of programs. Analysis of the
se examples shows the variability of secondary structure segment lengt
h and sequences of Greek keys even within one class. This variability
suggests that no single folding pathway is likely to fit all Greek key
structures.