1evd
From Proteopedia
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- | [[Image:1evd.jpg|left|200px]] | ||
- | + | ==NMR structure of CYANOBACTERIAL TOXIN, PHOSPHATASE-1/-2A INHIBITOR== | |
- | + | <StructureSection load='1evd' size='340' side='right'caption='[[1evd]]' scene=''> | |
- | | | + | == Structural highlights == |
- | | | + | <table><tr><td colspan='2'>[[1evd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EVD FirstGlance]. <br> |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1ZN:(2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-10-PHENYLDECA-4,6-DIENOIC+ACID'>1ZN</scene>, <scene name='pdbligand=ACB:3-METHYL-BETA-D-ASPARTIC+ACID'>ACB</scene>, <scene name='pdbligand=FGA:GAMMA-D-GLUTAMIC+ACID'>FGA</scene>, <scene name='pdbligand=MDH:N-METHYLDEHYDROBUTYRINE'>MDH</scene>, <scene name='pdbligand=PRD_000213:motuporin'>PRD_000213</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=1evd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1evd OCA], [https://pdbe.org/1evd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1evd RCSB], [https://www.ebi.ac.uk/pdbsum/1evd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1evd ProSAT]</span></td></tr> | |
- | + | </table> | |
- | + | <div style="background-color:#fffaf0;"> | |
- | + | == Publication Abstract from PubMed == | |
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A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets. | A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets. | ||
- | + | Comparison of the solution structures of microcystin-LR and motuporin.,Bagu JR, Sonnichsen FD, Williams D, Andersen RJ, Sykes BD, Holmes CF Nat Struct Biol. 1995 Feb;2(2):114-6. PMID:7749913<ref>PMID:7749913</ref> | |
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- | Comparison of the solution structures of microcystin-LR and motuporin., Bagu JR, Sonnichsen FD, Williams D, Andersen RJ, Sykes BD, Holmes CF | + | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 1evd" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Unidentified]] | ||
+ | [[Category: Bagu JR]] | ||
+ | [[Category: Sykes BD]] |
Current revision
NMR structure of CYANOBACTERIAL TOXIN, PHOSPHATASE-1/-2A INHIBITOR
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