1AQK

THREE-DIMENSIONAL STRUCTURE OF A HUMAN FAB WITH HIGH AFFINITY FOR TETANUS TOXOID

Summary for 1AQK

• Entry DOI: 10.2210/pdb1aqk/pdb
• Descriptor: FAB B7-15A2 (3 entities in total)
• Functional Keywords: human fab, anti-tetanus toxoid, high affinity, crystal packing motif, programming propensity to crystallize, immunoglobulin
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 46989.49

Authors

Faber, C.,Fan, Z.,Edmundson, A.B. (deposition date: 1997-07-30, release date: 1998-02-04, Last modification date: 2024-11-20)

Primary citation

Faber, C.,Shan, L.,Fan, Z.,Guddat, L.W.,Furebring, C.,Ohlin, M.,Borrebaeck, C.A.,Edmundson, A.B.
Three-dimensional structure of a human Fab with high affinity for tetanus toxoid.
Immunotechnology, 3:253-270, 1998

PubMed Abstract: The wide range of antibody specificity and affinity results from the differing shapes and chemical compositions of their binding sites. These shapes range from discrete grooves in antibodies elicited by linear oligomers of nucleotides and carbohydrates to shallow depressions or flat surfaces for accommodation of proteins, peptides and large organic compounds.

PubMed: 9530559
DOI: 10.1016/S1380-2933(97)10003-3

Experimental method

X-RAY DIFFRACTION (1.84 Å)