3obt

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(New page: '''Unreleased structure''' The entry 3obt is ON HOLD until Paper Publication Authors: Lee, K.K., Zong, Y., Jin, R. Description: Crystal structure of Botulinum neurotoxin serotype D lig...)
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'''Unreleased structure'''
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[[Image:3obt.jpg|left|200px]]
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The entry 3obt is ON HOLD until Paper Publication
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{{STRUCTURE_3obt| PDB=3obt | SCENE= }}
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Authors: Lee, K.K., Zong, Y., Jin, R.
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===Crystal structure of Botulinum neurotoxin serotype D ligand binding domain in complex with N-Acetylneuraminic acid===
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Description: Crystal structure of Botulinum neurotoxin serotype D ligand binding domain in complex with N-Acetylneuraminic acid
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 18 11:26:25 2010''
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{{ABSTRACT_PUBMED_20704566}}
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==About this Structure==
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3OBT is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OBT OCA].
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==Reference==
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<ref group="xtra">PMID:20704566</ref><references group="xtra"/>
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[[Category: Bontoxilysin]]
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[[Category: Clostridium botulinum]]
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[[Category: Jin, R.]]
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[[Category: Lee, K K.]]
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[[Category: Zong, Y.]]
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[[Category: Gangalioside]]
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[[Category: Hydrolase]]
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[[Category: Neurotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Sep 10 14:02:52 2010''

Revision as of 09:54, 10 September 2010

Image:3obt.jpg

Template:STRUCTURE 3obt

Crystal structure of Botulinum neurotoxin serotype D ligand binding domain in complex with N-Acetylneuraminic acid

Template:ABSTRACT PUBMED 20704566

About this Structure

3OBT is a 1 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

Reference

  • Strotmeier J, Lee K, Volker AK, Mahrhold S, Zong Y, Zeiser J, Zhou J, Pich A, Bigalke H, Binz T, Rummel A, Jin R. Botulinum neurotoxin serotype D attacks neurons via two carbohydrate binding sites in a ganglioside dependent manner. Biochem J. 2010 Aug 12. PMID:20704566 doi:10.1042/BJ20101042

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