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The important of crystallographic refinement for confident structural description, even at modest resolution, is demonstrated for N alpha A1,N epsilon B29-L,L-2,7-diaminosuberoyl (A2sb) insulin, a cross-linked insulin of low potency. The spatial arrangement of the cross-link itself can be described, and reliable estimates of the accuracy in atomic positions obtained. Comparison of invariant A2sb and native insulins shows a strong structural similarity, especially for the A chain surface residues and the dimer-forming residues of the B chain which have generally been strongly implicated in the receptor-binding region. Evidence from this analysis directs attention to the A chain, particularly the backbone, as being important in interactions with the membrane-bound receptor.

Evidence Concerning Insulin Activity from the Structure of a Cross-Linked Derivative