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The three-dimensional structure of the amaranth α-amylase inhibitor (AAI) adopts a knottin fold of abcabc topology. Upon binding to α-amylase, it adopts a more compact conformation characterized by an increased number of intramolecular hydrogen bonds, a decreased volume and in addition a trans to cis isomerization of Pro20. A systematic analysis of the 3-D structural databanks revealed that similar proteins and domains share with AAI the characteristic presence of proline residues, many ofdoi:10.1093/protein/14.9.639 pmid:11707609 fatcat:tdzihe4cmbhrnmu2ok4hxck5ee