1NUK

CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE

1NUK の概要

• エントリーDOI: 10.2210/pdb1nuk/pdb
• 分子名称: PROTEIN (TYROSINE-PROTEIN KINASE RECEPTOR EPH) (1 entity in total)
• 機能のキーワード: transferase, eph receptor tyrosine kinase
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P54763
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21139.88

構造登録者

Himanen, J.-P.,Henkemeyer, M.,Nikolov, D.B. (登録日: 1998-10-13, 公開日: 1999-10-13, 最終更新日: 2023-12-27)

主引用文献

Himanen, J.P.,Henkemeyer, M.,Nikolov, D.B.
Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2.
Nature, 396:486-491, 1998

PubMed Abstract: The Eph receptors, which bind a group of cell-membrane-anchored ligands known as ephrins, represent the largest subfamily of receptor tyrosine kinases (RTKs). They are predominantly expressed in the developing and adult nervous system and are important in contact-mediated axon guidance, axon fasciculation and cell migration. Eph receptors are unique among other RTKs in that they fall into two subclasses with distinct ligand specificities, and in that they can themselves function as ligands to activate bidirectional cell-cell signalling. We report here the crystal structure at 2.9 A resolution of the amino-terminal ligand-binding domain of the EphB2 receptor (also known as Nuk). The domain folds into a compact jellyroll beta-sandwich composed of 11 antiparallel beta-strands. Using structure-based mutagenesis, we have identified an extended loop that is important for ligand binding and class specificity. This loop, which is conserved within but not between Eph RTK subclasses, packs against the concave beta-sandwich surface near positions at which missense mutations cause signalling defects, localizing the ligand-binding region on the surface of the receptor.

PubMed: 9853759
DOI: 10.1038/24904

実験手法

X-RAY DIFFRACTION (2.9 Å)