1hoe
From Proteopedia
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- | [[Image:1hoe.png|left|200px]] | ||
- | + | ==CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A== | |
+ | <StructureSection load='1hoe' size='340' side='right'caption='[[1hoe]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1hoe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HOE 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]] 2Å</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=1hoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hoe OCA], [https://pdbe.org/1hoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hoe RCSB], [https://www.ebi.ac.uk/pdbsum/1hoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hoe ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/IAA_STRTE IAA_STRTE] Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases. Forms a tight stoichiometric 1:1 complex with alpha-amylase. | ||
+ | == 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/ho/1hoe_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=1hoe ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity. | ||
- | + | Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A.,Pflugrath JW, Wiegand G, Huber R, Vertesy L J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104<ref>PMID:3489104</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1hoe" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | < | + | </StructureSection> |
+ | [[Category: Large Structures]] | ||
[[Category: Streptomyces tendae]] | [[Category: Streptomyces tendae]] | ||
- | [[Category: Huber | + | [[Category: Huber R]] |
- | [[Category: Pflugrath | + | [[Category: Pflugrath JW]] |
- | [[Category: Wiegand | + | [[Category: Wiegand G]] |
- | + |
Current revision
CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A
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