Ion channels render nerve and muscle excitable. A typical channel prot
ein can mediate the passive transfer of millions of ions per second ac
ross the membrane. Thus, channels catalyse the transmembrane flux of i
ons, fulfilling criteria traditionally associated with enzymes. Is thi
s a semantic coincidence, or do channels and enzymes in fact rely upon
similar structural principles? A general answer remains elusive given
the paucity of crystallographic data on channels. Nevertheless, emerg
ing evidence points to fundamental similarities between the pores of c
hannels and the active sites of enzymes of resolved structure. Shared
features include narrow clefts lined by protein loops, and specific bi
nding of transition intermediates during catalysis. The often cited an
alogies between channels and enzymes might therefore reflect basic des
ign homologies.