Evolution favours the use of glycine-rich loops for nucleotide binding
in proteins. In the large family of protein kinases, the catalytic do
main of which has one of the highest degrees of conservation among all
known proteins, the structure of the nucleotide-binding site differs
from classical folds. We are now beginning to understand the multiple
functional roles of the glycine-rich sequence in protein kinases and s
ome of the structural constraints leading to its conservation.