2gsg
From Proteopedia
(New page: 200px<br /> <applet load="2gsg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gsg, resolution 2.10Å" /> '''Crystal structure o...) |
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caption="2gsg, resolution 2.10Å" /> | caption="2gsg, resolution 2.10Å" /> | ||
'''Crystal structure of the Fv fragment of a monoclonal antibody specific for poly-glutamine'''<br /> | '''Crystal structure of the Fv fragment of a monoclonal antibody specific for poly-glutamine'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GSG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2GSG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: poly-glutamine]] | [[Category: poly-glutamine]] | ||
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Revision as of 13:09, 23 January 2008
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Crystal structure of the Fv fragment of a monoclonal antibody specific for poly-glutamine
Overview
Huntington and related neurological diseases result from expansion of a, polyglutamine (polyQ) tract. The linear lattice model for the structure, and binding properties of polyQ proposes that both expanded and normal, polyQ tracts in the preaggregation state are random-coil structures but, that an expanded polyQ repeat contains a larger number of epitopes, recognized by antibodies or other proteins. The crystal structure of polyQ, bound to MW1, an antibody against polyQ, reveals that polyQ adopts an, extended, coil-like structure. Consistent with the linear lattice model, multimeric MW1 Fvs bind more tightly to longer than to shorter polyQ, tracts and, compared with monomeric Fv, bind expanded polyQ repeats with, higher apparent affinities. These results suggest a mechanism for the, toxicity of expanded polyQ and a strategy to link anti-polyQ compounds to, create high-avidity therapeutics.
About this Structure
2GSG is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model., Li P, Huey-Tubman KE, Gao T, Li X, West AP Jr, Bennett MJ, Bjorkman PJ, Nat Struct Mol Biol. 2007 May;14(5):381-7. Epub 2007 Apr 22. PMID:17450152
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