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http://purl.uniprot.org/citations/10400675http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10400675http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10400675http://www.w3.org/2000/01/rdf-schema#comment"alpha-Amylase inhibitor (AAI), a 32-residue miniprotein from the Mexican crop plant amaranth (Amaranthus hypochondriacus), is the smallest known alpha-amylase inhibitor and is specific for insect alpha-amylases (Chagolla-Lopez, A., Blanco-Labra, A., Patthy, A., Sanchez, R., and Pongor, S. (1994) J. Biol. Chem. 269, 23675-23680). Its disulfide topology was confirmed by Edman degradation, and its three-dimensional solution structure was determined by two-dimensional 1H NMR spectroscopy at 500 MHz. Structural constraints (consisting of 348 nuclear Overhauser effect interproton distances, 8 backbone dihedral constraints, and 9 disulfide distance constraints) were used as an input to the X-PLOR program for simulated annealing and energy minimization calculations. The final set of 10 structures had a mean pairwise root mean square deviation of 0.32 A for the backbone atoms and 1.04 A for all heavy atoms. The structure of AAI consists of a short triple-stranded beta-sheet stabilized by three disulfide bonds, forming a typical knottin or inhibitor cystine knot fold found in miniproteins, which binds various macromolecular ligands. When the first intercystine segment of AAI (sequence IPKWNR) was inserted into a homologous position of the spider toxin Huwentoxin I, the resulting chimera showed a significant inhibitory activity, suggesting that this segment takes part in enzyme binding."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.29.20473"xsd:string
http://purl.uniprot.org/citations/10400675http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.29.20473"xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Lu S."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Lu S."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Li F."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Li F."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Luo J."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Luo J."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Liang S."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Liang S."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Gu X."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Gu X."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Han R."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Han R."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Pongor S."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Pongor S."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Deng P."xsd:string
http://purl.uniprot.org/citations/10400675http://purl.uniprot.org/core/author"Deng P."xsd:string