3ton
From Proteopedia
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| - | [[ | + | ==Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase== |
| + | <StructureSection load='3ton' size='340' side='right' caption='[[3ton]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ton]] 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=3TON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TON FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3top|3top]]</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=3ton FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ton OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ton RCSB], [http://www.ebi.ac.uk/pdbsum/3ton 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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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Qin, X H.]] | [[Category: Qin, X H.]] | ||
Revision as of 06:37, 5 June 2014
Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase
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