Human EGFR
Human Epidermal Growth Factor Receptor (EGFR) is a transmembrane protein that plays a critical role in cell signaling and is frequently implicated in cancer.
Function
Human Epidermal Growth Factor Receptor (EGFR) is a transmembrane glycoprotein that is a member of the protein kinase superfamily. Binding of ligands such as epidermal growth factor (EGF) to EGFR induces receptor dimerization and tyrosine autophosphorylation, leading to cell proliferation. Mutations and amplifications of the EGFR gene are commonly associated with various cancers, particularly non-small-cell lung cancer, making it a key therapeutic target.
Structure
The human EGFR extracellular domain has been extensively studied through X-ray crystallography and cryo-electron microscopy. The structure reveals important insights into ligand binding and receptor dimerization mechanisms that are crucial for understanding EGFR signaling and developing targeted therapies.
Target Details
Protein Information
Protein Information
Organism: Homo sapiens (Human) Gene Name: EGFR Alternative Names: ErbB1, HER1 Protein Family: ErbB family receptor tyrosine kinases
Database References
Database References
UniProt ID: P00533 Gene ID: 1956 NCBI Reference: P00533-1 Protein Region: Leu 25 - Ser 645 (extracellular domain)
Structural Information
Structural Information
Molecular Weight: ~170 kDa (full-length), ~70 kDa (extracellular domain) Structure: Four domains (I-IV) with ligand binding and dimerization interfaces Key Features: Signal peptide, ligand binding domains, transmembrane region, kinase domain PDB Structures: Multiple structures available including 1IVO