1B4F

OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN

1B4F の概要

• エントリーDOI: 10.2210/pdb1b4f/pdb
• 分子名称: EPHB2 (2 entities in total)
• 機能のキーワード: sam domain, eph receptor, signal transduction, oligomer
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 75214.18

構造登録者

Thanos, C.D.,Goodwill, K.E.,Bowie, J.U. (登録日: 1998-12-20, 公開日: 1999-02-16, 最終更新日: 2024-02-07)

主引用文献

Thanos, C.D.,Goodwill, K.E.,Bowie, J.U.
Oligomeric structure of the human EphB2 receptor SAM domain.
Science, 283:833-836, 1999

PubMed Abstract: The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.

PubMed: 9933164
DOI: 10.1126/science.283.5403.833

実験手法

X-RAY DIFFRACTION (1.95 Å)