Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nahoum V, Farisei F, Le-Berre-Anton V, Egloff MP, Rouge P, Poerio E, Payan F. 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. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):360-2. Epub 1999, Jan 1. PMID:10089450 doi:10.1107/S0907444998010701
