2gsg: Difference between revisions
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[[Image:2gsg.jpg|left|200px]] | [[Image:2gsg.jpg|left|200px]] | ||
'''Crystal structure of the Fv fragment of a monoclonal antibody specific for poly-glutamine''' | {{Structure | ||
|PDB= 2gsg |SIZE=350|CAPTION= <scene name='initialview01'>2gsg</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the Fv fragment of a monoclonal antibody specific for poly-glutamine''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2GSG is a [ | 2GSG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17450152 17450152] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: poly-glutamine]] | [[Category: poly-glutamine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:08:28 2008'' | ||
Revision as of 18:08, 20 March 2008
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Crystal structure of the Fv fragment of a monoclonal antibody specific for poly-glutamine
OverviewOverview
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 StructureAbout this Structure
2GSG is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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