1hoe: Difference between revisions
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==CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A== | ==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=''> | <StructureSection load='1hoe' size='340' side='right'caption='[[1hoe]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hoe]] is a 1 chain structure with sequence from [ | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ho/1hoe_consurf.spt"</scriptWhenChecked> | <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/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 31: | Line 32: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces tendae]] | ||
[[Category: | [[Category: Huber R]] | ||
[[Category: | [[Category: Pflugrath JW]] | ||
[[Category: | [[Category: Wiegand G]] | ||
Latest revision as of 11:30, 6 November 2024
CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467ACRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A
Structural highlights
FunctionIAA_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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