1MFE
RECOGNITION OF A CELL-SURFACE OLIGO-SACCHARIDE OF PATHOGENIC SALMONELLA BY AN ANTIBODY FAB FRAGMENT
Summary for 1MFE
Entry DOI | 10.2210/pdb1mfe/pdb |
Descriptor | IGG1-LAMBDA SE155-4 FAB (LIGHT CHAIN), IGG1-LAMBDA SE155-4 FAB (HEAVY CHAIN), alpha-D-galactopyranose-(1-2)-[alpha-D-Abequopyranose-(1-3)]alpha-D-mannopyranose, ... (4 entities in total) |
Functional Keywords | immunoglobulin |
Biological source | Mus musculus (house mouse) More |
Total number of polymer chains | 2 |
Total formula weight | 47151.51 |
Authors | Cygler, M. (deposition date: 1993-10-25, release date: 1994-01-31, Last modification date: 2024-10-30) |
Primary citation | Cygler, M.,Rose, D.R.,Bundle, D.R. Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. Science, 253:442-445, 1991 Cited by PubMed Abstract: The 2.05 angstrom (A) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 A deep by 7 A wide) in an entropy-assisted association (association constant = 2.05 x 10(5) liters per mole, enthalpy = -20.5 +/- 1.7 kilojoules per mole, and temperature times entropy = +10.0 +/- 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine the antigen conformation adopted in the bound state. PubMed: 1713710PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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