7T0K

Crystal structure of S25-2 Fab Unliganded 4

Summary for 7T0K

• Entry DOI: 10.2210/pdb7t0k/pdb
• Related: 7T0F 7T0G 7T0H 7T0I 7T0J
• Descriptor: S25-2 Fab light chain, S25-2 Fab heavy chain, IODIDE ION, ... (4 entities in total)
• Functional Keywords: antibody, fab, carbohydrate, induced fit, conformational selection, immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 8
• Total formula weight: 198014.51

Authors

Legg, M.S.G.,Blackler, R.J.,Evans, S.V. (deposition date: 2021-11-29, release date: 2022-04-20, Last modification date: 2024-10-09)

Primary citation

Blackler, R.J.,Muller-Loennies, S.,Pokorny-Lehrer, B.,Legg, M.S.G.,Brade, L.,Brade, H.,Kosma, P.,Evans, S.V.
Antigen binding by conformational selection in near-germline antibodies.
J.Biol.Chem., 298:101901-101901, 2022

PubMed Abstract: Conformational flexibility in antibody-combining sites has been hypothesized to facilitate polyspecificity toward multiple unique epitopes and enable the limited germline repertoire to match an overwhelming diversity of potential antigens; however, elucidating the mechanisms of antigen recognition by flexible antibodies has been understandably challenging. Here, multiple liganded and unliganded crystal structures of the near-germline anticarbohydrate antibodies S25-2 and S25-39 are reported, which reveal an unprecedented diversity of complementarity-determining region H3 conformations in apparent equilibrium. These structures demonstrate that at least some germline or near-germline antibodies are flexible entities sensitive to their chemical environments, with conformational selection available as an evolved mechanism that preserves the inherited ability to recognize common pathogens while remaining adaptable to new threats.

PubMed: 35395245
DOI: 10.1016/j.jbc.2022.101901

Experimental method

X-RAY DIFFRACTION (2 Å)