1Q9W

S45-18 Fab pentasaccharide bisphosphate complex

Summary for 1Q9W

• Entry DOI: 10.2210/pdb1q9w/pdb
• Related: 1q9k 1q9l 1q9o 1q9q 1q9r 1q9t 1q9v
• Descriptor: S45-18 Fab (IgG1k) light chain, S45-18 Fab (IgG1k) heavy chain, 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)-3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)-3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-6)-2-amino-2-deoxy-4-O-phosphono-alpha-D-glucopyranose-(1-6)-2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: antigen-binding fragment, fab, anti-cabohydrate, anti-lps, antibody, immunoglobulin, kdo, protein-carbohydrate complex, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 4
• Total formula weight: 99463.76

Authors

Nguyen, H.P.,Seto, N.O.,MacKenzie, C.R.,Brade, L.,Kosma, P.,Brade, H.,Evans, S.V. (deposition date: 2003-08-26, release date: 2004-01-27, Last modification date: 2023-08-16)

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

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: 14625588
DOI: 10.1038/nsb1014

Experimental method

X-RAY DIFFRACTION (1.75 Å)