1EMT

FAB ANTIBODY FRAGMENT OF AN C60 ANTIFULLERENE ANTIBODY

Summary for 1EMT

• Entry DOI: 10.2210/pdb1emt/pdb
• Descriptor: IGG ANTIBODY (LIGHT CHAIN), IGG ANTIBODY (HEAVY CHAIN) (3 entities in total)
• Functional Keywords: anti-fullerene antibody, nanotubes, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 46456.67

Authors

Braden, B.C.,Goldbaum, F.A.,Chen, B.-X.,Erlanger, B.F.,Kirschner, A.N.,Wilson, S.R. (deposition date: 2000-03-17, release date: 2000-11-01, Last modification date: 2024-10-09)

Primary citation

Braden, B.C.,Goldbaum, F.A.,Chen, B.X.,Kirschner, A.N.,Wilson, S.R.,Erlanger, B.F.
X-ray crystal structure of an anti-Buckminsterfullerene antibody fab fragment: biomolecular recognition of C(60).
Proc.Natl.Acad.Sci.USA, 97:12193-12197, 2000

PubMed Abstract: 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.

PubMed: 11035793
DOI: 10.1073/pnas.210396197

Experimental method

X-RAY DIFFRACTION (2.25 Å)