3top
From Proteopedia
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- | [[ | + | ==Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose== |
+ | <StructureSection load='3top' size='340' side='right' caption='[[3top]], [[Resolution|resolution]] 2.88Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3top]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TOP FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACR:ALPHA-ACARBOSE'>ACR</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ton|3ton]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MGAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3top FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3top OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3top RCSB], [http://www.ebi.ac.uk/pdbsum/3top PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Human maltase-glucoamylase (MGAM) hydrolyzes linear alpha-1,4-linked oligosaccharide substrates, playing a crucial role in the production of glucose in the human lumen and acting as an efficient drug target for type 2 diabetes and obesity. The amino- and carboxyl-terminal portions of MGAM (MGAM-N and MGAM-C) carry out the same catalytic reaction but have different substrate specificities. In this study, we report crystal structures of MGAM-C alone at a resolution of 3.1 A, and in complex with its inhibitor acarbose at a resolution of 2.9 A. Structural studies, combined with biochemical analysis, revealed that a segment of 21 amino acids in the active site of MGAM-C forms additional sugar subsites (+ 2 and + 3 subsites), accounting for the preference for longer substrates of MAGM-C compared with that of MGAM-N. Moreover, we discovered that a single mutation of Trp1251 to tyrosine in MGAM-C imparts a novel catalytic ability to digest branched alpha-1,6-linked oligosaccharides. These results provide important information for understanding the substrate specificity of alphaglucosidases during the process of terminal starch digestion, and for designing more efficient drugs to control type 2 diabetes or obesity. | ||
- | + | Structural insight into substrate specificity of human intestinal maltase-glucoamylase.,Ren L, Qin X, Cao X, Wang L, Bai F, Bai G, Shen Y Protein Cell. 2011 Oct;2(10):827-36. Epub 2011 Nov 6. PMID:22058037<ref>PMID:22058037</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Qin, X H.]] | [[Category: Qin, X H.]] |
Revision as of 06:15, 5 June 2014
Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose
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