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3bae

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{{STRUCTURE_3bae| PDB=3bae | SCENE= }}
{{STRUCTURE_3bae| PDB=3bae | SCENE= }}
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'''Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)'''
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===Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)===
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==Overview==
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Alzheimer's disease (AD) is the most common form of dementia. Amyloid-beta (A beta) peptide, generated by proteolytic cleavage of the amyloid precursor protein, is central to AD pathogenesis. Most pharmaceutical activity in AD research has focused on A beta, its generation and clearance from the brain. In particular, there is much interest in immunotherapy approaches with a number of anti-A beta antibodies in clinical trials. We have developed a monoclonal antibody, called WO2, which recognises the A beta peptide. To this end, we have determined the three-dimensional structure, to near atomic resolution, of both the antibody and the complex with its antigen, the A beta peptide. The structures reveal the molecular basis for WO2 recognition and binding of A beta. The A beta peptide adopts an extended, coil-like conformation across its major immunodominant B-cell epitope between residues 2 and 8. We have also studied the antibody-bound A beta peptide in the presence of metals known to affect its aggregation state and show that WO2 inhibits these interactions. Thus, antibodies that target the N-terminal region of A beta, such as WO2, hold promise for therapeutic development.
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==About this Structure==
==About this Structure==
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[[Category: Immunotherapy]]
[[Category: Immunotherapy]]
[[Category: Wo2]]
[[Category: Wo2]]
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Revision as of 12:59, 27 July 2008

Image:3bae.png

Template:STRUCTURE 3bae

Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)

Template:ABSTRACT PUBMED 18237744

About this Structure

3BAE is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope., Miles LA, Wun KS, Crespi GA, Fodero-Tavoletti MT, Galatis D, Bagley CJ, Beyreuther K, Masters CL, Cappai R, McKinstry WJ, Barnham KJ, Parker MW, J Mol Biol. 2008 Mar 14;377(1):181-92. Epub 2008 Jan 30. PMID:18237744

Page seeded by OCA on Sun Jul 27 15:59:32 2008

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