4NZU
Crystal structure of the primary monoclonal antibody 13PL Fab' from a multiple myeloma patient
Summary for 4NZU
Entry DOI | 10.2210/pdb4nzu/pdb |
Related | 4NZR 4NZT |
Descriptor | 13PL heavy chain, 13PL light chain, GLYCEROL, ... (5 entities in total) |
Functional Keywords | antibody fab, multiple myeloma, primary antibody, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 47084.17 |
Authors | Zhu, X.,Wilson, I.A. (deposition date: 2013-12-12, release date: 2014-02-19, Last modification date: 2024-10-30) |
Primary citation | Grover, R.K.,Zhu, X.,Nieusma, T.,Jones, T.,Boero, I.,MacLeod, A.S.,Mark, A.,Niessen, S.,Kim, H.J.,Kong, L.,Assad-Garcia, N.,Kwon, K.,Chesi, M.,Smider, V.V.,Salomon, D.R.,Jelinek, D.F.,Kyle, R.A.,Pyles, R.B.,Glass, J.I.,Ward, A.B.,Wilson, I.A.,Lerner, R.A. A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union. Science, 343:656-661, 2014 Cited by PubMed Abstract: We report the discovery of a broadly reactive antibody-binding protein (Protein M) from human mycoplasma. The crystal structure of the ectodomain of transmembrane Protein M differs from other known protein structures, as does its mechanism of antibody binding. Protein M binds with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the κ and λ light chains. Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens. Similar to the other immunoglobulin-binding proteins such as Protein A, Protein M as well as its orthologs in other Mycoplasma species could become invaluable reagents in the antibody field. PubMed: 24503852DOI: 10.1126/science.1246135 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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