1SZH

Crystal Structure of C. elegans HER-1

Summary for 1SZH

• Entry DOI: 10.2210/pdb1szh/pdb
• Descriptor: Her-1 protein, ACETATE ION (3 entities in total)
• Functional Keywords: extended 3-10 helix; left-handed anti-parallel 4-helix bundle, overhand 3-helix bundle, signaling protein
• Biological source: Caenorhabditis elegans
• Cellular location: Secreted: P34704
• Total number of polymer chains: 2
• Total formula weight: 37088.86

Authors

Hamaoka, B.Y.,Dann III, C.E.,Geisbrecht, B.V.,Leahy, D.J. (deposition date: 2004-04-05, release date: 2004-08-10, Last modification date: 2024-10-30)

Primary citation

Hamaoka, B.Y.,Dann III, C.E.,Geisbrecht, B.V.,Leahy, D.J.
Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A.
Proc.Natl.Acad.Sci.USA, 101:1673-11678, 2004

PubMed 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.

PubMed: 15289613
DOI: 10.1073/pnas.0402559101

Experimental method

X-RAY DIFFRACTION (1.5 Å)