Recognition of a Cell-Surface Oligosaccharide of Pathogenic Salmonella by an Antibody Fab Fragment

The 2.05 angstrom (Å) 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 that are features of transport and other, car...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1991-07, Vol.253 (5018), p.442-445
Hauptverfasser: Cygler, Miroslaw, Rose, David R., Bundle, David R.
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Rose, David R.
Bundle, David R.
description The 2.05 angstrom (Å) 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 that are features of transport and other, carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 Å deep by 7 Å wide) in an entropy-assisted association (association constant = 2.05 × 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
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Study of affinity. Antigen presentation</topic><topic>Antigens</topic><topic>Atoms</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Conformation</topic><topic>Carbohydrate Sequence</topic><topic>Carbohydrates</topic><topic>Crystal structure</topic><topic>Epitopes</topic><topic>Epitopes - chemistry</topic><topic>Fundamental and applied biological sciences. 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A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 Å deep by 7 Å wide) in an entropy-assisted association (association constant = 2.05 × 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</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>1713710</pmid><doi>10.1126/science.1713710</doi><tpages>4</tpages></addata></record>
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subjects Amino Acid Sequence
Antibodies
Antigen-Antibody Complex
Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation
Antigens
Atoms
Biological and medical sciences
Carbohydrate Conformation
Carbohydrate Sequence
Carbohydrates
Crystal structure
Epitopes
Epitopes - chemistry
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humans
Hydrogen bonds
Immune complexes
Immunoglobulin Fab Fragments - chemistry
Immunoglobulin Fab Fragments - immunology
Immunoglobulin G - classification
Immunoglobulin G - immunology
Lipopolysaccharides - chemistry
Lipopolysaccharides - immunology
Models, Molecular
Molecular immunology
Molecular Sequence Data
Molecular structure
Molecules
Oligosaccharides
Oligosaccharides - chemistry
Oligosaccharides - immunology
Protein Conformation
Salmonella - immunology
Salmonella - pathogenicity
Science
Sugars
X-ray crystallography
title Recognition of a Cell-Surface Oligosaccharide of Pathogenic Salmonella by an Antibody Fab Fragment
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