1d0h: Difference between revisions

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[[Image:1d0h.png|left|200px]]
==THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH N-ACETYL-GALACTOSAMINE==
<StructureSection load='1d0h' size='340' side='right' caption='[[1d0h]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d0h]] 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=1D0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D0H FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
<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=1d0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d0h RCSB], [http://www.ebi.ac.uk/pdbsum/1d0h PDBsum]</span></td></tr>
<table>
== 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/d0/1d0h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1d0h|  PDB=1d0h  |  SCENE=  }}
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>


===THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH N-ACETYL-GALACTOSAMINE===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_10722735}}
 
==About this Structure==
[[1d0h]] 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=1D0H OCA].


==See Also==
==See Also==
*[[Tetanus toxin|Tetanus toxin]]
*[[Tetanus toxin|Tetanus toxin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:010722735</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Clostridium tetani]]
[[Category: Clostridium tetani]]
[[Category: Black, I.]]
[[Category: Black, I.]]

Revision as of 12:08, 27 August 2014

THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH N-ACETYL-GALACTOSAMINETHE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH N-ACETYL-GALACTOSAMINE

Structural highlights

1d0h is a 1 chain structure with sequence from Clostridium tetani. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

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 PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Emsley P, Fotinou C, Black I, Fairweather NF, Charles IG, Watts C, Hewitt E, Isaacs NW. The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding. J Biol Chem. 2000 Mar 24;275(12):8889-94. PMID:10722735

1d0h, resolution 2.10Å

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