NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.

Abstract

The three-dimensional structure of the 56 residue polypeptide Apis mellifera chymotrypsin/cathepsin G inhibitor 1 (AMCI-1) isolated from honey bee hemolymph was calculated based on 730 experimental NMR restraints. It consists of two approximately perpendicular beta-sheets, several turns, and a long exposed loop that includes the protease binding site. The… (More)

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Cite this paper

@article{Cierpicki2000NMRSS, title={NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.}, author={Tomasz Cierpicki and Jacek Bania and Jacek Otlewski}, journal={Protein science : a publication of the Protein Society}, year={2000}, volume={9 5}, pages={976-84} }