3top

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (17:33, 1 November 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3top.jpg|left|200px]]
 
-
<!--
+
==Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose==
-
The line below this paragraph, containing "STRUCTURE_3top", creates the "Structure Box" on the page.
+
<StructureSection load='3top' size='340' side='right'caption='[[3top]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3top]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3TOP FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.881&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900007:alpha-acarbose'>PRD_900007</scene></td></tr>
-
{{STRUCTURE_3top| PDB=3top | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3top FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3top OCA], [https://pdbe.org/3top PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3top RCSB], [https://www.ebi.ac.uk/pdbsum/3top PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3top ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MGA_HUMAN MGA_HUMAN] May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing.
 +
<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.
-
===Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose===
+
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>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3top" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_22058037}}, adds the Publication Abstract to the page
+
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 22058037 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_22058037}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
[[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].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:022058037</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Qin, X H.]]
+
[[Category: Large Structures]]
-
[[Category: Ren, L M.]]
+
[[Category: Qin XH]]
-
[[Category: Shen, Y.]]
+
[[Category: Ren LM]]
-
[[Category: Hydrolase-hydrolase inhibitor complex]]
+
[[Category: Shen Y]]
-
[[Category: Membrane]]
+

Current revision

Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose

PDB ID 3top

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3top"
Personal tools