1MOX

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

Summary for 1MOX

• Entry DOI: 10.2210/pdb1mox/pdb
• Related: 1IGR 1M6B 2TGF
• Descriptor: Epidermal Growth Factor Receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose, Transforming Growth Factor alpha, ... (11 entities in total)
• Functional Keywords: egfr, receptor, complex, growth factor, transferase-growth factor complex, transferase/growth factor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 127948.54

Authors

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. (deposition date: 2002-09-10, release date: 2003-09-10, Last modification date: 2020-07-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)