1viw

TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX

spinqualitylabelsall models 1viw, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1viw is a 2 chain structure with sequence from Phaseolus vulgaris and Tenebrio molitor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: CA, CL, NAG, PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LEA1_PHAVU Lectin and alpha-amylase inhibitor. Acts as a defensive protein against insects.[:] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The alpha-amylase from Tenebrio molitor larvae (TMA) has been crystallized in complex with the alpha-amylase inhibitor (alpha-AI) from the bean Phaseolus vulgaris. A molecular-replacement solution of the structure was obtained using the refined pig pancreatic alpha-amylase (PPA) and alpha-AI atomic coordinates as starting models. The structural analysis showed that although TMA has the typical structure common to alpha-amylases, large deviations from the mammalian alpha-amylase models occur in the loops. Despite these differences in the interacting loops, the bean inhibitor is still able to inhibit both the insect and mammalian alpha-amylase. A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor.,Nahoum V, Farisei F, Le-Berre-Anton V, Egloff MP, Rouge P, Poerio E, Payan F Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):360-2. Epub 1999, Jan 1. PMID:10089450 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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