4hix

Crystal structure of a humanised 3D6 Fab bound to amyloid beta peptide

spinqualitylabelsall models 4hix, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hix is a 3 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.204Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease IGHG1_HUMAN Defects in IGHG1 are a cause of multiple myeloma (MM) [MIM: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 IGHG1_HUMAN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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