Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A
| Autor: | Brian V. Geisbrecht, Brent Y. Hamaoka, Charles E. Dann, Daniel J. Leahy |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Protein Conformation
Protein structure X-Ray Diffraction Animals Amino Acid Sequence Binding site Caenorhabditis elegans Proteins Selenomethionine Integral membrane protein Peptide sequence Caenorhabditis elegans chemistry.chemical_classification Multidisciplinary Binding Sites biology Chinese hamster ovary cell Membrane Proteins Biological Sciences biology.organism_classification Cell biology Amino acid Biochemistry Membrane protein chemistry Amino Acid Substitution Crystallization Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 101(32) |
| ISSN: | 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|