Alpha-glucosidase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='3a4a' size='340' side='right' caption='Structure of yeast isomaltase complex with glucose | + | <StructureSection load='3a4a' size='340' side='right' caption='Structure of yeast isomaltase complex with α-D-glucose and Ca+2 ion (green) (PDB code [[3a4a]]).' scene='59/596427/Cv/1'> |
== Function == | == Function == | ||
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AGS deficiency is the cause of Pompe Disease. AGS inhibitors are used as anti-diabetic drugs and can potentially prevent the fusion of HIV and hepatitis B virus to cells. | AGS deficiency is the cause of Pompe Disease. AGS inhibitors are used as anti-diabetic drugs and can potentially prevent the fusion of HIV and hepatitis B virus to cells. | ||
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| + | == Structural highlights == | ||
| + | <scene name='59/596427/Cv/2'>α-D-glucose binding site</scene> (PDB code [[3a4a]]). | ||
</StructureSection> | </StructureSection> | ||
Revision as of 12:24, 6 December 2015
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3D structures of α-glucosidase
Updated on 06-December-2015
References
- ↑ Gloster TM, Turkenburg JP, Potts JR, Henrissat B, Davies GJ. Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora. Chem Biol. 2008 Oct 20;15(10):1058-67. Epub 2008 Oct 9. PMID:18848471 doi:10.1016/j.chembiol.2008.09.005
