2ait
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2ait.png|left|200px]] | ||
- | + | ==DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY== | |
- | + | <StructureSection load='2ait' size='340' side='right'caption='[[2ait]]' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2ait]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AIT FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 9 models</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=2ait FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ait OCA], [https://pdbe.org/2ait PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ait RCSB], [https://www.ebi.ac.uk/pdbsum/2ait PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ait 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/ai/2ait_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=2ait ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The complete three-dimensional structure of the alpha-amylase inhibitor Tendamistat in aqueous solution was determined by 1H nuclear magnetic resonance and distance geometry calculations using the program DISMAN. Compared to an earlier, preliminary determination of the polypeptide backbone conformation, stereo-specific assignments were obtained for 41 of the 89 prochiral groups in the protein, and a much more extensive set of experimental constraints was collected, including 842 distance constraints from nuclear Overhauser effects and over 100 supplementary constraints from spin-spin coupling constants and the identification of intramolecular hydrogen bonds. The complete protein molecule, including the amino acid side-chains is characterized by a group of nine structures corresponding to the results of the nine DISMAN calculations with minimal residual error functions. The average of the pairwise minimal root-mean-square distances among these nine structures is 0.85 A for the polypeptide backbone, and 1.52 A for all the heavy atoms. The procedures used for the structure determination are described and a detailed analysis is presented of correlations between the experimental input data and the precision of the structure determination. | ||
- | + | Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry.,Kline AD, Braun W, Wuthrich K J Mol Biol. 1988 Dec 5;204(3):675-724. PMID:3265733<ref>PMID:3265733</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2ait" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
- | + | ||
- | + | ||
- | == | + | |
- | + | ||
- | [[Category: | + | |
[[Category: Streptomyces tendae]] | [[Category: Streptomyces tendae]] | ||
- | [[Category: Billeter | + | [[Category: Billeter M]] |
- | [[Category: Braun | + | [[Category: Braun W]] |
- | [[Category: Guntert | + | [[Category: Guntert P]] |
- | [[Category: Kline | + | [[Category: Kline AD]] |
- | [[Category: Wuthrich | + | [[Category: Wuthrich K]] |
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- | + |
Current revision
DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY
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