12E8

2E8 FAB FRAGMENT

Summary for 12E8

• Entry DOI: 10.2210/pdb12e8/pdb
• Descriptor: IGG1-KAPPA 2E8 FAB (LIGHT CHAIN), IGG1-KAPPA 2E8 FAB (HEAVY CHAIN) (3 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 4
• Total formula weight: 94839.15

Authors

Rupp, B.,Trakhanov, S. (deposition date: 1998-03-14, release date: 1998-08-05, Last modification date: 2024-10-16)

Primary citation

Trakhanov, S.,Parkin, S.,Raffai, R.,Milne, R.,Newhouse, Y.M.,Weisgraber, K.H.,Rupp, B.
Structure of a monoclonal 2E8 Fab antibody fragment specific for the low-density lipoprotein-receptor binding region of apolipoprotein E refined at 1.9 A.
Acta Crystallogr.,Sect.D, null:122-128, 1999

PubMed Abstract: The crystal structure of the Fab fragment of 2E8, the monoclonal IgG1,kappa antibody specific for the low-density lipoprotein (LDL) receptor-binding region of apolipoprotein E (apoE), has been solved by molecular replacement and refined at 1.9 A resolution (PDB entry 12E8). Two 2E8 Fab molecules in the asymmetric unit are related by noncrystallographic symmetry and are hydrogen bonded through a beta-sheet-like intermolecular contact between the heavy-chain complementarity-determining regions 3 (CDRH3) of each molecule. The structure has been refined to an R value of 0.22 (Rfree = 0.27). The initially ill-defined heavy-chain constant domain (CH1) of 2E8 has been retraced with the aid of automatic refinement, confirming the beta-sheet tracing independently of any starting models. As a resolution better than 2 A is not common for Fab fragments, this model represents a well defined Fab structure and should prove useful in MR solution of other Fab fragments. Furthermore, in the absence of an LDL-receptor structure, the homology of the 2E8 CDRH2 to the ligand-binding domain of the LDL receptor has been exploited to model the apoE-LDL-receptor interaction.

PubMed: 10089402
DOI: 10.1107/S090744499800938X

Experimental method

X-RAY DIFFRACTION (1.9 Å)