Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A

AUTOR(ES)

Hamaoka, Brent Y.

FONTE

National Academy of Sciences

RESUMO

HER-1 is a secreted protein that promotes male development in the nematode Caenorhabditis elegans. HER-1 inhibits the function of TRA-2A, a multipass integral membrane protein thought to serve as its receptor. We report here the 1.5-Å crystal structure of HER-1. The structure was solved by the multiwavelength anomalous diffraction method by using selenomethionyl-substituted HER-1 produced in Chinese hamster ovary cells. The HER-1 structure consists of two all-helical domains and is not closely homologous to any known structure. Sites of amino acid substitutions known to impair HER-1 function were mapped on the HER-1 structure and classified according to the likely mechanism by which they affect HER-1 activity. A subset of these and other amino acid substitutions on the HER-1 surface were assayed for their ability to disrupt interactions between HER-1 and TRA-2A-expressing cells, and a localized region on the HER-1 surface important for mediating this interaction was identified.

Documentos Relacionados

• Negative regulation of male development in Caenorhabditis elegans by a protein–protein interaction between TRA-2A and FEM-3
• Proteolysis in Caenorhabditis elegans sex determination: cleavage of TRA-2A by TRA-3
• A Novel Dominant Transformer Allele of the Sex-Determining Gene Her-1 of Caenorhabditis Elegans
• Sequenced Alleles of the Caenorhabditis Elegans Sex-Determining Gene Her-1 Include a Novel Class of Conditional Promoter Mutations
• The TRA-1 transcription factor binds TRA-2 to regulate sexual fates in Caenorhabditis elegans