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1FL3

CRYSTAL STRUCTURE OF THE BLUE FLUORESCENT ANTIBODY (19G2) IN COMPLEX WITH STILBENE HAPTEN AT 277K

Summary for 1FL3
Entry DOI10.2210/pdb1fl3/pdb
DescriptorBLUE FLUORESCENT ANTIBODY (19G2)-HEAVY CHAIN, BLUE FLUORESCENT ANTIBODY (19G2)-LIGHT CHAIN, 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID, ... (4 entities in total)
Functional Keywordsimmunoglobulin fold, immune system
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains4
Total formula weight91181.90
Authors
Stevens, R.C.,Beuscher IV, A.E. (deposition date: 2000-08-11, release date: 2000-11-01, Last modification date: 2024-10-30)
Primary citationSimeonov, A.,Matsushita, M.,Juban, E.A.,Thompson, E.H.,Hoffman, T.Z.,Beuscher IV, A.E.,Taylor, M.J.,Wirsching, P.,Rettig, W.,McCusker, J.K.,Stevens, R.C.,Millar, D.P.,Schultz, P.G.,Lerner, R.A.,Janda, K.D.
Blue-fluorescent antibodies.
Science, 290:307-313, 2000
Cited by
PubMed Abstract: The forte of catalytic antibodies has resided in the control of the ground-state reaction coordinate. A principle and method are now described in which antibodies can direct the outcome of photophysical and photochemical events that take place on excited-state potential energy surfaces. The key component is a chemically reactive optical sensor that provides a direct report of the dynamic interplay between protein and ligand at the active site. To illustrate the concept, we used a trans-stilbene hapten to elicit a panel of monoclonal antibodies that displayed a range of fluorescent spectral behavior when bound to a trans-stilbene substrate. Several antibodies yielded a blue fluorescence indicative of an excited-state complex or "exciplex" between trans-stilbene and the antibody. The antibodies controlled the isomerization coordinate of trans-stilbene and dynamically coupled this manifold with an active-site residue. A step was taken toward the use of antibody-based photochemical sensors for diagnostic and clinical applications.
PubMed: 11030644
DOI: 10.1126/science.290.5490.307
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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