1emt

From Proteopedia

Revision as of 07:22, 18 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1emt, resolution 2.25Å

Drag the structure with the mouse to rotate

FAB ANTIBODY FRAGMENT OF AN C60 ANTIFULLERENE ANTIBODY

Overview

We have prepared a monoclonal Buckminsterfullerene specific antibody and, report the sequences of its light and heavy chains. We also show, by x-ray, crystallographic analysis of the Fab fragment and by model building, that, the fullerene binding site is formed by the interface of the antibody, light and heavy chains. Shape-complementary clustering of hydrophobic, amino acids, several of which participate in putative stacking, interactions with fullerene, form the binding site. Moreover, an induced, fit mechanism appears to participate in the fullerene binding process., Affinity of the antibody-fullerene complex is 22 nM as measured by, competitive binding. These findings should be applicable not only to the, use of antibodies to assay and direct potential fullerene-based drug, design but could also lead to new methodologies for the production of, fullerene derivatives and nanotubes as well.

About this Structure

1EMT is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of an anti-Buckminsterfullerene antibody fab fragment: biomolecular recognition of C(60)., Braden BC, Goldbaum FA, Chen BX, Kirschner AN, Wilson SR, Erlanger BF, Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):12193-7. PMID:11035793

Page seeded by OCA on Sun Nov 18 09:29:17 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools