ArticleProceedings of the National Academy of Sciences of the United States of America2004
Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Bridging the Gap between Sequence and Structure Classifications of Proteins with AlphaFold Models.Journal of molecular biology · 2024Article
- Transcriptional profiles in Strongyloides stercoralis males reveal deviations from the Caenorhabditis sex determination model.Scientific reports · 2021Article
- Structure of the RECK CC domain, an evolutionary anomaly.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues.The Journal of biological chemistry · 2016Article
- Somatic sex determination in Caenorhabditis elegans is modulated by SUP-26 repression of tra-2 translation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Chapter 3. Caenorhabditis nematodes as a model for the adaptive evolution of germ cells.Current topics in developmental biology · 2009Review
- Comparative genetics of sex determination: masculinizing mutations in Caenorhabditis briggsae.Genetics · 2008Article
- A sensitized genetic background reveals evolution near the terminus of the Caenorhabditis germline sex determination pathway.Evolution & developmentArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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-A 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.