1SZH

Crystal Structure of C. elegans HER-1

1SZH の概要

• エントリーDOI: 10.2210/pdb1szh/pdb
• 分子名称: Her-1 protein, ACETATE ION (3 entities in total)
• 機能のキーワード: extended 3-10 helix; left-handed anti-parallel 4-helix bundle, overhand 3-helix bundle, signaling protein
• 由来する生物種: Caenorhabditis elegans
• 細胞内の位置: Secreted: P34704
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37088.86

構造登録者

Hamaoka, B.Y.,Dann III, C.E.,Geisbrecht, B.V.,Leahy, D.J. (登録日: 2004-04-05, 公開日: 2004-08-10, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.5 Å)