Three-dimensional Structure Of An Fv From A Human IgM Immunoglobulin

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dc.contributor.author Fan, Zhoufu en_US
dc.contributor.author Shan, L en_US
dc.contributor.author Guddat, Lw en_US
dc.contributor.author He, Xm en_US
dc.contributor.author Gray, Wr en_US
dc.contributor.author Raison, Robert en_US
dc.contributor.author Edmundson, Allen en_US
dc.contributor.editor en_US
dc.date.accessioned 2011-02-07T06:20:20Z
dc.date.available 2011-02-07T06:20:20Z
dc.date.issued 1992 en_US
dc.identifier 2006014217 en_US
dc.identifier.citation Fan Zhoufu et al. 1992, 'Three-dimensional Structure Of An Fv From A Human IgM Immunoglobulin', Academic Press Ltd, vol. 228, no. 1, pp. 188-207. en_US
dc.identifier.issn 0022-2836 en_US
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/13272
dc.description.abstract An IgM(?) immunoglobulin from a patient (Pot) with Waldenstrom's macroglobulinemia was hydrolyzed with pepsin to release a fragment consisting of the `variable? (V) domains of the light and heavy chains plus eight residue `tails? from the `constant? (C) domains. The crystal structure of this fragment was determined at 2.3 ? resolution by molecular replacement and crystallographic refinement methods. When examined separately, the light chain component closely resembles another human ? chain (Rei) in both the ?-pleated sheet regions and the `hypervariable? loops. The conserved pleated sheets in the heavy chain are similar to those in the human Kol IgG1 protein, but the third hypervariable loop in particular is different from that in any immunoglobulin structure described to date. As in the Kol protein, this loop blocks the access to any internal active site along the light-heavy chain interface. Unlike the Kol protein, however, the loop does not protrude beyond the boundaries of a conventional antigen combining site. Instead, it forms a very compact structure, which fills almost all residual space between the domains. This is an example of one dominant complementarity-determining region (CDR) essentially negating the diversity possible with five other CDRs in the two chains. Ordered water molecules are associated with light chain constituents along the interface, but not with CDR3 of the heavy chain. In screening exercises the Pot IgM failed to bind a wide variety of peptides. Together, the results suggest that ligand binding can only occur on external surfaces of the protein. These surfaces carry a limited number of side chains usually assigned to CDRs in more typical antibodies. en_US
dc.language en_US
dc.publisher Academic Press Ltd en_US
dc.relation.isbasedon http://dx.doi.org/10.1016/0022-2836(92)90500-J en_US
dc.title Three-dimensional Structure Of An Fv From A Human IgM Immunoglobulin en_US
dc.parent Journal of Molecular Biology en_US
dc.journal.volume 228 en_US
dc.journal.number 1 en_US
dc.publocation London, UK en_US
dc.identifier.startpage 188 en_US
dc.identifier.endpage 207 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 060107 en_US
dc.personcode 0000022731 en_US
dc.personcode 0000035036 en_US
dc.personcode 0000035037 en_US
dc.personcode 0000035038 en_US
dc.personcode 0000035039 en_US
dc.personcode 890404 en_US
dc.personcode 0000024041 en_US
dc.percentage 100 en_US
dc.classification.name Enzymes en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity ISI:A1992JZ52000016 en_US
dc.description.keywords Antibody-antigen Complex; Crystallographic Refinement; Macromolecular Structures; Fab Fragment; Light Chain; Lambda-type; X-ray; Resolution; Binding; Dimer en_US


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