3bae

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{{Seed}}
 
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[[Image:3bae.png|left|200px]]
 
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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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The line below this paragraph, containing "STRUCTURE_3bae", creates the "Structure Box" on the page.
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<StructureSection load='3bae' size='340' side='right'caption='[[3bae]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3bae]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BAE FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.593&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bae OCA], [https://pdbe.org/3bae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bae RCSB], [https://www.ebi.ac.uk/pdbsum/3bae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bae ProSAT]</span></td></tr>
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{{STRUCTURE_3bae| PDB=3bae | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A2NHM3_MOUSE A2NHM3_MOUSE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/3bae_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bae ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)===
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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<ref>PMID:18237744</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3bae" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18237744}}, adds the Publication Abstract to the page
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*[[Amyloid precursor protein 3D structures|Amyloid precursor protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18237744 is the PubMed ID number.
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_18237744}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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3BAE 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=3BAE OCA].
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18237744 18237744]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Crespi GA]]
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[[Category: Crespi, G A.]]
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[[Category: Miles LA]]
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[[Category: Miles, L A.]]
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[[Category: Parker MW]]
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[[Category: Parker, M W.]]
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[[Category: Wun KS]]
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[[Category: Wun, K S.]]
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[[Category: Abeta]]
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[[Category: Alzheimer's disease]]
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[[Category: Amyloid beta peptide]]
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[[Category: App]]
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[[Category: Fab]]
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[[Category: Immune system]]
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[[Category: Immunotherapy]]
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[[Category: Wo2]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:59:32 2008''
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Current revision

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

PDB ID 3bae

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OCA

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