1f11
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(New page: 200px<br /> <applet load="1f11" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f11, resolution 3.0Å" /> '''F124 FAB FRAGMENT FR...)
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Revision as of 07:22, 18 November 2007
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F124 FAB FRAGMENT FROM A MONOCLONAL ANTI-PRES2 ANTIBODY
Overview
The crystal structure of the Fab fragment from the monoclonal anti-preS2, antibody F124 (IgG1,kappa) has been solved by molecular replacement and, refined at 3.0 A resolution. The Fab crystallizes with two independent, molecules in the asymmetric unit. F124 recognizes an epitope contained, within the preS2 segment between residues 120 and 132 of the surface, antigen of hepatitis B virus. The antibody shows a high affinity for the, glycan N-linked to Asn123, but it also cross-reacts with the, non-glycosylated peptide fragment 120-132. Although crystallization was, performed in the presence of an eightfold excess of the cross-reactive, peptide, no evidence for the ligand was found in the antigen-binding site, which is close to a neighbouring molecule in the crystal lattice. The, antigen-binding site has a groove-like topology which is modulated with, pocket-like cavities. It is characterized by a large number of tyrosine, and aspartate residues. The importance of germ-line mutations at the, binding site is discussed.
About this Structure
1F11 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the Fab fragment from F124, a monoclonal antibody specific for hepatitis B surface antigen., Saul FA, Vulliez-Le Normand B, Passafiume M, Riottot MM, Bentley GA, Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):945-51. PMID:10944330
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