2wah

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(New page: '''Unreleased structure''' The entry 2wah is ON HOLD until Paper Publication Authors: Crispin, M., Bowden, T.A., Coles, C.H., Harlos, K., Aricescu, A.R., Harvey, D.J., Stuart, D.I., Jon...)
Current revision (15:49, 13 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2wah is ON HOLD until Paper Publication
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==Crystal Structure of an IgG1 Fc Glycoform (Man9GlcNAc2)==
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<StructureSection load='2wah' size='340' side='right'caption='[[2wah]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2wah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WAH 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]] 2.51&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=2wah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wah OCA], [https://pdbe.org/2wah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wah RCSB], [https://www.ebi.ac.uk/pdbsum/2wah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wah ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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.
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== Function ==
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[https://www.uniprot.org/uniprot/IGHG1_HUMAN IGHG1_HUMAN]
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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/wa/2wah_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2wah 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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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.
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Authors: Crispin, M., Bowden, T.A., Coles, C.H., Harlos, K., Aricescu, A.R., Harvey, D.J., Stuart, D.I., Jones, E.Y.
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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<ref>PMID:19236877</ref>
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Description: Crystal Structure of an IgG1 Fc Glycoform (Man9GlcNAc2)
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 25 09:18:54 2009''
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<div class="pdbe-citations 2wah" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Aricescu AR]]
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[[Category: Bowden TA]]
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[[Category: Coles CH]]
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[[Category: Crispin M]]
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[[Category: Harlos K]]
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[[Category: Harvey DJ]]
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[[Category: Jones EY]]
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[[Category: Stuart DI]]

Current revision

Crystal Structure of an IgG1 Fc Glycoform (Man9GlcNAc2)

PDB ID 2wah

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