4HGW

Crystal structure of S25-2 in complex with a 5,6-dehydro-Kdo disaccharide

Summary for 4HGW

• Entry DOI: 10.2210/pdb4hgw/pdb
• Descriptor: Antibody Fab fragment, light chain, Antibody Fab fragment, heavy chain, 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-4)-prop-2-en-1-yl 3,5-dideoxy-alpha-D-threo-oct-5-en-2-ulopyranosidonic acid, ... (5 entities in total)
• Functional Keywords: antibody, lps, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 2
• Total formula weight: 48965.10

Authors

Brooks, C.L.,Evans, S.V. (deposition date: 2012-10-08, release date: 2013-01-09, Last modification date: 2024-11-20)

Primary citation

Brooks, C.L.,Wimmer, K.,Kosma, P.,Muller-Loennies, S.,Brade, L.,Brade, H.,Evans, S.V.
Exploring the cross-reactivity of S25-2: complex with a 5,6-dehydro-Kdo disaccharide.
Acta Crystallogr.,Sect.F, 69:2-5, 2013

PubMed Abstract: The near-germline antibody S25-2 exhibits a remarkable cross-reactivity for oligosaccharides containing the bacterial lipopolysaccharide carbohydrate 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo). The recent synthesis of a variety of Kdo analogues permits a detailed structural analysis of the importance of specific interactions in antigen recognition by S25-2. The Kdo disaccharide analogue Kdo-(2→4)-5,6-dehydro-Kdo lacks a 5-OH group on the second Kdo residue and has been cocrystallized with S25-2. The structure reveals that the modification of the Kdo residue at position 5 results in a rearrangement of intramolecular hydrogen bonds in the antigen that allows it to assume a novel conformation in the antibody-combining site. The cross-reactive binding of S25-2 to this synthetic ligand highlights the adaptability of this antibody to non-natural synthetic analogues.

PubMed: 23295476
DOI: 10.1107/S1744309112047422

Experimental method

X-RAY DIFFRACTION (1.65 Å)