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Protein Engineering, Vol. 13, No. 6, 391-394, June 2000
© 2000 Oxford University Press

Communications

Sequence annotation of nuclear receptor ligand-binding domains by automated homology modeling

C.Jan J. Françoijs1, Jan P.G. Klomp2 and Ronald M.A. Knegtel3,4

1 Laboratory of Biochemistry, Wageningen Agricultural University, Dreijenlaan 3, 6703 HA Wageningen, 2 Target Discovery Unit and 3 Department of Molecular Design and Informatics, NV Organon,P.O. Box 20, 5340 BH Oss, The Netherlands

The quality of three-dimensional homology models derived from protein sequences provides an independent measure of the suitability of a protein sequence for a certain fold. We have used automated homology modeling and model assessment tools to identify putative nuclear hormone receptor ligand-binding domains in the genome of Caenorhabditis elegans. Our results indicate that the availability of multiple crystal structures is crucial to obtaining useful models in this receptor family. The majority of annotated mammalian nuclear hormone receptors could be assigned to a ligand-binding domain fold by using the best model derived from any of four template structures. This strategy also assigned the ligand-binding domain fold to a number of C.elegans sequences without prior annotation. Interestingly, the retinoic acid receptor crystal structure contributed most to the number of sequences that could be assigned to a ligand-binding domain fold. Several causes for this can be suggested, including the high quality of this protein structure in terms of our assessment tools, similarity between the biological function or ligand of this receptor and the modeled genes and gene duplication in C.elegans.


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