1RHF

Crystal Structure of human Tyro3-D1D2

1RHF の概要

• エントリーDOI: 10.2210/pdb1rhf/pdb
• 分子名称: Tyrosine-protein kinase receptor TYRO3, ZINC ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: axl/tyro3 family, cellular adhesion, ligand-independent dimerization, mutational analysis, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: Q06418
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40062.07

構造登録者

Heiring, C.,Dahlback, B.,Muller, Y.A. (登録日: 2003-11-14, 公開日: 2004-03-23, 最終更新日: 2024-10-16)

主引用文献

Heiring, C.,Dahlback, B.,Muller, Y.A.
Ligand recognition and homophilic interactions in Tyro3: structural insights into the Axl/Tyro3 receptor tyrosine kinase family.
J.Biol.Chem., 279:6952-6958, 2004

PubMed Abstract: The receptor Tyro3 together with Axl and Mer form the Axl/Tyro3 family of receptor tyrosine kinases. Members of this family play essential roles in spermatogenesis, immunoregulation, and phagocytosis. Gas6, the product of growth arrest-specific gene, activates the kinase activity of all three receptors. Here, we report the first biochemical and structural characterization of a member of this family, namely of a fragment spanning the two N-terminal Ig domains of the extracellular part of human Tyro3. Its ligand binding specificity profile is identical to the activation profile of the native receptor. The 1.95-A crystal structure suggests a common ligand-binding site in this receptor family located at the interface of the Ig domains and unusually rich in cis-prolines. Furthermore, both in the crystal and in solution we observed the ligand-independent dimerization of the receptor fragment. This homophilic interaction emphasizes previous functional reports, which hinted that in addition to signal transduction, members of this family of receptors might participate in cell adhesion.

PubMed: 14623883
DOI: 10.1074/jbc.M311750200

実験手法

X-RAY DIFFRACTION (1.96 Å)