4hix
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a humanised 3D6 Fab bound to amyloid beta peptide== | |
| + | <StructureSection load='4hix' size='340' side='right'caption='[[4hix]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hix]] 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=4HIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HIX FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.204Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hix OCA], [https://pdbe.org/4hix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hix RCSB], [https://www.ebi.ac.uk/pdbsum/4hix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hix ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/IGHG1_HUMAN IGHG1_HUMAN] Defects in IGHG1 are a cause of multiple myeloma (MM) [MIM:[https://omim.org/entry/254500 254500]. MM is a malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. Note=A chromosomal aberration involving IGHG1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus. Translocation t(11;14)(q13;q32) with CCND1; translocation t(4;14)(p16.3;q32.3) with FGFR3; translocation t(6;14)(p25;q32) with IRF4. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IGHG1_HUMAN IGHG1_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bapineuzumab is a humanized antibody developed by Pfizer and Johnson & Johnson targeting the amyloid (Abeta) plaques that underlie Alzheimer's disease neuropathology. Here we report the crystal structure of a Fab-Abeta peptide complex that reveals Bapineuzumab surprisingly captures Abeta in a monomeric helical conformation at the N-terminus. Microscale thermophoresis suggests that the Fab binds soluble Abeta(1-40) with a K(D) of 89 (+/-9) nM. The structure explains the antibody's exquisite selectivity for particular Abeta species and why it cannot recognize N-terminally modified or truncated Abeta peptides. | ||
| - | + | Bapineuzumab captures the N-terminus of the Alzheimer's disease amyloid-beta peptide in a helical conformation.,Miles LA, Crespi GA, Doughty L, Parker MW Sci Rep. 2013 Feb 18;3:1302. doi: 10.1038/srep01302. PMID:23416764<ref>PMID:23416764</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4hix" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Crespi GAN]] | ||
| + | [[Category: Miles LA]] | ||
| + | [[Category: Parker MW]] | ||
Current revision
Crystal structure of a humanised 3D6 Fab bound to amyloid beta peptide
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