1MOX

Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha

1MOX の概要

• エントリーDOI: 10.2210/pdb1mox/pdb
• 関連するPDBエントリー: 1IGR 1M6B 2TGF
• 分子名称: Epidermal Growth Factor Receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose, Transforming Growth Factor alpha, ... (11 entities in total)
• 機能のキーワード: egfr, receptor, complex, growth factor, transferase-growth factor complex, transferase/growth factor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 127948.54

構造登録者

Garrett, T.P.J.,McKern, N.M.,Lou, M.,Elleman, T.C.,Adams, T.E.,Lovrecz, G.O.,Zhu, H.-J.,Walker, F.,Frenkel, M.J.,Hoyne, P.A.,Jorissen, R.N.,Nice, E.C.,Burgess, A.W.,Ward, C.W. (登録日: 2002-09-10, 公開日: 2003-09-10, 最終更新日: 2024-11-13)

主引用文献

Garrett, T.P.J.,McKern, N.M.,Lou, M.,Elleman, T.C.,Adams, T.E.,Lovrecz, G.O.,Zhu, H.-J.,Walker, F.,Frenkel, M.J.,Hoyne, P.A.,Jorissen, R.N.,Nice, E.C.,Burgess, A.W.,Ward, C.W.
Crystal Structure of a Truncated Epidermal Growth Factor Receptor Extracellular Domain Bound to Transforming Growth Factor alpha
Cell(Cambridge,Mass.), 110:763-773, 2002

PubMed Abstract: We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha. TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues. The results indicate how EGFR family members can bind a family of highly variable ligands. In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule. There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor. Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.

PubMed: 12297049
DOI: 10.1016/S0092-8674(02)00940-6

実験手法

X-RAY DIFFRACTION (2.5 Å)