Summary for 3T77
| Entry DOI | 10.2210/pdb3t77/pdb |
| Descriptor | S25-2 FAB (IGG1K) light chain, S25-2 FAB (IGG1K) heavy chain, 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)-prop-2-en-1-yl 3-deoxy-alpha-D-manno-oct-2-ulopyranosidonic acid, ... (6 entities in total) |
| Functional Keywords | antigen-binding fragment, fab, anti-carbohydrate, anti-lps, antibody, immunoglobulin, kdo, immune system |
| Biological source | Mus musculus (mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 49184.55 |
| Authors | Nguyen, H.P.,Seto, N.O.,Mackenzie, C.R.,Brade, L.,Kosma, P.,Brade, H.,Evans, S.V. (deposition date: 2011-07-29, release date: 2011-08-24, Last modification date: 2024-10-16) |
| Primary citation | Nguyen, H.P.,Seto, N.O.,MacKenzie, C.R.,Brade, L.,Kosma, P.,Brade, H.,Evans, S.V. Germline antibody recognition of distinct carbohydrate epitopes. Nat.Struct.Biol., 10:1019-1025, 2003 Cited by PubMed Abstract: High-resolution structures reveal how a germline antibody can recognize a range of clinically relevant carbohydrate epitopes. The germline response to a carbohydrate immunogen can be critical to survivability, with selection for antibody gene segments that both confer protection against common pathogens and retain the flexibility to adapt to new disease organisms. We show here that antibody S25-2 binds several distinct inner-core epitopes of bacterial lipopolysaccharides (LPSs) by linking an inherited monosaccharide residue binding site with a subset of complementarity-determining regions (CDRs) of limited flexibility positioned to recognize the remainder of an array of different epitopes. This strategy allows germline antibodies to adapt to different epitopes while minimizing entropic penalties associated with the immobilization of labile CDRs upon binding of antigen, and provides insight into the link between the genetic origin of individual CDRs and their respective roles in antigen recognition. PubMed: 14625588DOI: 10.1038/nsb1014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.739 Å) |
Structure validation
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