1jhk
Crystal structure of the anti-estradiol antibody 57-2
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OverviewOverview
The crystal structure of a Fab fragment of an anti-17beta-estradiol, antibody 57-2 was determined in the absence and presence of the steroid, ligand, 17beta-estradiol (E2), at 2.5 and 2.15-A resolutions, respectively. The antibody binds the steroid in a deep hydrophobic pocket, formed at the interface between the variable domains. No major structural, rearrangements take place upon ligand binding; however, a large part of, the heavy chain variable domain near the binding pocket is unusually, flexible and is partly stabilized when the steroid is bound. The nonpolar, steroid skeleton of E2 is recognized by a number of hydrophobic, interactions, whereas the two hydroxyl groups of E2 are hydrogen-bonded to, the protein. Especially, the 17-hydroxyl group of E2 is recognized by an, intricate hydrogen bonding network in which the 17-hydroxyl itself forms a, rare four-center hydrogen bond with three polar amino acids; this hydrogen, bonding arrangement accounts for the low cross-reactivity of the antibody, with other estrogens such as estrone. The CDRH3 loop plays a prominent, role in ligand binding. All the complementarity-determining regions of the, light chain make direct contacts with the steroid, even CDRL2, which is, rarely directly involved in the binding of haptens.
About this StructureAbout this Structure
1JHK is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a recombinant anti-estradiol Fab fragment in complex with 17beta -estradiol., Lamminmaki U, Kankare JA, J Biol Chem. 2001 Sep 28;276(39):36687-94. Epub 2001 Jul 12. PMID:11451948
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