ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
The α-amylase from Tenebrio molitor larvae (TMA) has been crystallized in complex with the α-amylase inhibitor (α-AI) from the bean Phaseolus vulgaris. A molecular-replacement solution of the structure was obtained using the refined pig pancreatic α-amylase (PPA) and α-AI atomic coordinates as starting models. The structural analysis showed that although TMA has the typical structure common to α-amylases, large deviations from the mammalian α-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 α-amylase.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444998010701
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