1IKO

CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN

1IKO の概要

• エントリーDOI: 10.2210/pdb1iko/pdb
• 分子名称: EPHRIN-B2, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: greek key, glycosylation, signaling protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20484.98

構造登録者

Toth, J.,Cutforth, T.,Gelinas, A.D.,Bethoney, K.A.,Bard, J.,Harrison, C.J. (登録日: 2001-05-03, 公開日: 2002-05-03, 最終更新日: 2024-11-06)

主引用文献

Toth, J.,Cutforth, T.,Gelinas, A.D.,Bethoney, K.A.,Bard, J.,Harrison, C.J.
Crystal structure of an ephrin ectodomain.
Dev.Cell, 1:83-92, 2001

PubMed Abstract: Eph receptor tyrosine kinases and their membrane-associated ligands, the ephrins, are essential regulators of axon guidance, cell migration, segmentation, and angiogenesis. There are two classes of vertebrate ephrin ligands which have distinct binding specificities for their cognate receptors. Multimerization of the ligands is required for receptor activation, and ephrin ligands themselves signal intracellularly upon binding Eph receptors. We have determined the structure of the extracellular domain of mouse ephrin-B2. The ephrin ectodomain is an eight-stranded beta barrel with topological similarity to plant nodulins and phytocyanins. Based on the structure, we have identified potential surface determinants of Eph/ephrin binding specificity and a ligand dimerization region. The high sequence similarity among ephrin ectodomains indicates that all ephrins may be modeled upon the ephrin-B2 structure presented here.

PubMed: 11703926
DOI: 10.1016/S1534-5807(01)00002-8

実験手法

X-RAY DIFFRACTION (1.92 Å)