12e8

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=12e8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=12e8 OCA], [http://www.ebi.ac.uk/pdbsum/12e8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=12e8 RCSB]</span>
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Revision as of 15:27, 30 March 2008


PDB ID 12e8

Drag the structure with the mouse to rotate
, resolution 1.90Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



2E8 FAB FRAGMENT


Overview

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.

About this Structure

12E8 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

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., Trakhanov S, Parkin S, Raffai R, Milne R, Newhouse YM, Weisgraber KH, Rupp B, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):122-8. Epub 1999, Jan 1. PMID:10089402

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