1PLG

EVIDENCE FOR THE EXTENDED HELICAL NATURE OF POLYSACCHARIDE EPITOPES. THE 2.8 ANGSTROMS RESOLUTION STRUCTURE AND THERMODYNAMICS OF LIGAND BINDING OF AN ANTIGEN BINDING FRAGMENT SPECIFIC FOR ALPHA-(2->8)-POLYSIALIC ACID

Summary for 1PLG

• Entry DOI: 10.2210/pdb1plg/pdb
• Descriptor: IGG2A=KAPPA= (3 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P01865
• Total number of polymer chains: 2
• Total formula weight: 46760.03

Authors

Evans, S.V.,Sigurskjold, B.W.,Jennings, H.J.,Brisson, J.-R.,Tse, W.C.,To, R.,Altman, E.,Frosch, M.,Weisgerber, C.,Kratzin, H.,Klebert, S.,Vaesen, M.,Bitter-Suermann, D.,Rose, D.R.,Young, N.M.,Bundle, D.R. (deposition date: 1995-04-24, release date: 1996-04-03, Last modification date: 2024-10-16)

Primary citation

Evans, S.V.,Sigurskjold, B.W.,Jennings, H.J.,Brisson, J.R.,To, R.,Tse, W.C.,Altman, E.,Frosch, M.,Weisgerber, C.,Kratzin, H.D.,Klebert, S.,Vaesen, M.,Bitter-Suermann, D.,Rose, D.R.,Young, N.M.,Bundle, D.R.
Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 A resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for alpha-(2-->8)-polysialic acid.
Biochemistry, 34:6737-6744, 1995

PubMed Abstract: The antigen binding fragment from an IgG2a kappa murine monoclonal antibody with specificity for alpha-(2-->8)-linked sialic acid polymers has been prepared and crystallized in the absence of hapten. Crystals were grown by vapor diffusion equilibrium with 16-18% polyethylene glycol 4000 solutions. The structure was solved by molecular replacement methods and refined to a conventional R factor of 0.164 for data to 2.8 A. The binding site is observed to display a shape and distribution of charges that is complementary to that of the predicted conformation of the oligosaccharide epitope. A thermodynamic description of ligand binding has been compiled for oligosaccharides ranging in length from 9 to 41 residues, and the data for the largest ligand has been used in a novel way to estimate the size of the antigen binding site. A model of antigen binding is presented that satisfies this thermodynamic data, as well as a previously reported requirement of conformational specificity of the oligosaccharide. X-ray crystallographic and thermodynamic evidence are consistent with a binding site that accommodates at least eight sialic acid residues.

PubMed: 7538787
DOI: 10.1021/bi00020a019

Experimental method

X-RAY DIFFRACTION (2.8 Å)