2r0z

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[[Image:2r0z.gif|left|200px]]
[[Image:2r0z.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2r0z |SIZE=350|CAPTION= <scene name='initialview01'>2r0z</scene>, resolution 2.096&Aring;
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The line below this paragraph, containing "STRUCTURE_2r0z", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2r0z| PDB=2r0z | SCENE= }}
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|RELATEDENTRY=[[2ipt|2IPT]], [[2ipu|2IPU]], [[2iqa|2IQA]], [[2iq9|2IQ9]], [[2r0w|2R0W]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0z OCA], [http://www.ebi.ac.uk/pdbsum/2r0z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2r0z RCSB]</span>
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}}
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'''PFA1 FAB complexed with GripI peptide fragment'''
'''PFA1 FAB complexed with GripI peptide fragment'''
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[[Category: Dealwis, C.]]
[[Category: Dealwis, C.]]
[[Category: Gardberg, A S.]]
[[Category: Gardberg, A S.]]
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[[Category: alzheimer disease]]
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[[Category: Alzheimer disease]]
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[[Category: amyloid]]
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[[Category: Amyloid]]
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[[Category: immune system]]
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[[Category: Immune system]]
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[[Category: immunoglobulin]]
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[[Category: Immunoglobulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:03:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:55:24 2008''
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Revision as of 13:03, 4 May 2008

Template:STRUCTURE 2r0z

PFA1 FAB complexed with GripI peptide fragment


Overview

Amyloid aggregates of the amyloid-beta (Abeta) peptide are implicated in the pathology of Alzheimer's disease. Anti-Abeta monoclonal antibodies (mAbs) have been shown to reduce amyloid plaques in vitro and in animal studies. Consequently, passive immunization is being considered for treating Alzheimer's, and anti-Abeta mAbs are now in phase II trials. We report the isolation of two mAbs (PFA1 and PFA2) that recognize Abeta monomers, protofibrils, and fibrils and the structures of their antigen binding fragments (Fabs) in complex with the Abeta(1-8) peptide DAEFRHDS. The immunodominant EFRHD sequence forms salt bridges, hydrogen bonds, and hydrophobic contacts, including interactions with a striking WWDDD motif of the antigen binding fragments. We also show that a similar sequence (AKFRHD) derived from the human protein GRIP1 is able to cross-react with both PFA1 and PFA2 and, when cocrystallized with PFA1, binds in an identical conformation to Abeta(1-8). Because such cross-reactivity has implications for potential side effects of immunotherapy, our structures provide a template for designing derivative mAbs that target Abeta with improved specificity and higher affinity.

About this Structure

2R0Z is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Molecular basis for passive immunotherapy of Alzheimer's disease., Gardberg AS, Dice LT, Ou S, Rich RL, Helmbrecht E, Ko J, Wetzel R, Myszka DG, Patterson PH, Dealwis C, Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15659-64. Epub 2007 Sep 25. PMID:17895381 Page seeded by OCA on Sun May 4 16:03:21 2008

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