12e8
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="12e8" size="450" color="white" frame="true" align="right" spinBox="true" caption="12e8, resolution 1.90Å" /> '''2E8 FAB FRAGMENT'''...)
Next diff →
Revision as of 07:17, 18 November 2007
|
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
Page seeded by OCA on Sun Nov 18 09:24:46 2007
