2wah | pdb_00002wah

CRYSTAL STRUCTURE OF AN IGG1 FC GLYCOFORM (MAN9GLCNAC2)

spinqualitylabelsall models 2wah, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wah is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, MAN, NAG Related: 1e4k, 1t83, 1h3u, 1h3v, 1oqx, 1fc1, 2rcs, 1aqk, 2iwg, 1d5b, 1d5i, 1i7z, 2j6e, 1h3y, 1d6v, 1fcc, 1h3w, 1dn2, 1t89, 1h3t, 1aj7, 1l6x, 1bey Resources: FirstGlance, OCA, RCSB, PDBsum 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding. Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions.,Crispin M, Bowden TA, Coles CH, Harlos K, Aricescu AR, Harvey DJ, Stuart DI, Jones EY J Mol Biol. 2009 Apr 17;387(5):1061-6. Epub 2009 Feb 21. PMID:19236877 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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