1dfq

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[[Image:1dfq.png|left|200px]]
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==THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACID==
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<StructureSection load='1dfq' size='340' side='right' caption='[[1dfq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dfq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DFQ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d0h|1d0h]], [[1af9|1af9]], [[1a8d|1a8d]], [[1diw|1diw]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dfq RCSB], [http://www.ebi.ac.uk/pdbsum/1dfq PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/1dfq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The entry of tetanus neurotoxin into neuronal cells proceeds through the initial binding of the toxin to gangliosides on the cell surface. The carboxyl-terminal fragment of the heavy chain of tetanus neurotoxin contains the ganglioside-binding site, which has not yet been fully characterized. The crystal structures of native H(C) and of H(C) soaked with carbohydrates reveal a number of binding sites and provide insight into the possible mode of ganglioside binding.
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{{STRUCTURE_1dfq| PDB=1dfq | SCENE= }}
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The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.,Emsley P, Fotinou C, Black I, Fairweather NF, Charles IG, Watts C, Hewitt E, Isaacs NW J Biol Chem. 2000 Mar 24;275(12):8889-94. PMID:10722735<ref>PMID:10722735</ref>
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===THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACID===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_10722735}}
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==About this Structure==
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[[1dfq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFQ OCA].
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==See Also==
==See Also==
*[[Tetanus toxin|Tetanus toxin]]
*[[Tetanus toxin|Tetanus toxin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:010722735</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Clostridium tetani]]
[[Category: Clostridium tetani]]
[[Category: Tentoxilysin]]
[[Category: Tentoxilysin]]

Revision as of 06:46, 4 September 2014

THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACID

1dfq, resolution 2.60Å

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