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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 DOI10.2210/pdb1plg/pdb
DescriptorIGG2A=KAPPA= (3 entities in total)
Functional Keywordsimmunoglobulin
Biological sourceMus musculus (house mouse)
More
Cellular locationCell membrane; Single-pass membrane protein (Potential): P01865
Total number of polymer chains2
Total formula weight46760.03
Authors
Primary citationEvans, 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
Cited by
PubMed: 7538787
DOI: 10.1021/bi00020a019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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