1u30: Difference between revisions

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-[[Image:1u30.png|left|200px]]
-{{STRUCTURE_1u30|  PDB=1u30  |  SCENE=  }}
+==In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam==
+<StructureSection load='1u30' size='340' side='right'caption='[[1u30]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1u30]] is a 1 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=1U30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U30 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOX:(2S,3S,4R,5R)-6-(HYDROXYAMINO)-2-(HYDROXYMETHYL)-2,3,4,5-TETRAHYDROPYRIDINE-3,4,5-TRIOL'>GOX</scene>, <scene name='pdbligand=LAG:MALTOSYL-ALPHA+(1,4)-(Z,3S,4S,5R,6R)-3,4,5-TRIHYDROXY-6-HYDROXYMETHYL-PIPERIDIN-2-ONE+OXIME'>LAG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u30 OCA], [https://pdbe.org/1u30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u30 RCSB], [https://www.ebi.ac.uk/pdbsum/1u30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u30 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AMYP_HUMAN AMYP_HUMAN]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u3/1u30_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u30 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of alpha-amylases based upon autoglucosylation of known alpha-glucosidase inhibitors is presented. This concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, d-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of human pancreatic alpha-amylase with a K(i) value of 18 mm to a trisaccharide analogue with a K(i) value of 25 mum. The three-dimensional structure of this complex was determined by x-ray crystallography and represents the first such structure determined with this class of inhibitors in any alpha-glycosidase. This approach to the discovery and structural analysis of amylase inhibitors should be generally applicable to other endoglucosidases and readily adaptable to a high throughput format.
-===In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam===
+In situ extension as an approach for identifying novel alpha-amylase inhibitors.,Numao S, Damager I, Li C, Wrodnigg TM, Begum A, Overall CM, Brayer GD, Withers SG J Biol Chem. 2004 Nov 12;279(46):48282-91. Epub 2004 Aug 10. PMID:15304511<ref>PMID:15304511</ref>
-{{ABSTRACT_PUBMED_15304511}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1u30" style="background-color:#fffaf0;"></div>
-[[1u30]] is a 1 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=1U30 OCA].
 ==See Also==
-*[[Alpha-Amylase|Alpha-Amylase]]
+*[[Amylase 3D structures|Amylase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:015304511</ref><references group="xtra"/>
+__TOC__
-[[Category: Alpha-amylase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Begum, A.]]
+[[Category: Large Structures]]
-[[Category: Brayer, G D.]]
+[[Category: Begum A]]
-[[Category: Damager, I.]]
+[[Category: Brayer GD]]
-[[Category: Li, C.]]
+[[Category: Damager I]]
-[[Category: Numao, S.]]
+[[Category: Li C]]
-[[Category: Overall, C M.]]
+[[Category: Numao S]]
-[[Category: Withers, S G.]]
+[[Category: Overall CM]]
-[[Category: Wrodnigg, T M.]]
+[[Category: Withers SG]]
-[[Category: Acarbose]]
+[[Category: Wrodnigg TM]]
-[[Category: Enzyme mechanism]]
-[[Category: Glucosidase]]
-[[Category: Glycosidase]]
-[[Category: Human pancreatic alpha-amylase]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]