4NZT

Crystal structure of the antibody-binding region of Protein M (Protein M TD) in complex with anti-infleunza hemagglutinin antibody CR9114 Fab

Summary for 4NZT

• Entry DOI: 10.2210/pdb4nzt/pdb
• Related: 4FQH 4NZR 4NZU
• Descriptor: Protein M TD, CR9114 heavy chain, CR9114 light chain, ... (4 entities in total)
• Functional Keywords: leucine-rich repeat, broad antibody-binding, block antibody-antigen union, variable region, protein binding-immune system complex, protein binding/immune system
• Biological source: Mycoplasma genitalium; More
• Cellular location: Membrane; Single-pass membrane protein (Potential): P47523
• Total number of polymer chains: 3
• Total formula weight: 94190.02

Authors

Zhu, X.,Wilson, I.A. (deposition date: 2013-12-12, release date: 2014-02-19, Last modification date: 2024-10-16)

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

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: 24503852
DOI: 10.1126/science.1246135

Experimental method

X-RAY DIFFRACTION (2.497 Å)