Secondary structural and “active site” momologies between nerve growth factor and insulin

Secondary structural elements, α-helix, β-sheet and turns, of nerve growth factor (NGF) were predicted by the method of Chou and Fasman. Analysis of the prediction results showed the presence of domain structure in NGF; the second half of the polypeptide chain showed a secondary structural “pattern” very similar to the first half. Comparison of the secondary structure of NGF and proinsulin showed significant homology between the B-chain, which has the “active site”, and NGF^25–54 The homology is reinforced by the identification of a pentapeptide sequence in NGF which is very similar to the “active site” sequence of insluin essential for receptor binding and agonist activity. The present alignment of insulin and NGF is however different from that proposed earlier on the basis of sequence data alone.