1emt
From Proteopedia
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| , resolution 2.25Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 30 20:05:45 2008
