Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.
The structure was published by Ferguson, K.M., Berger, M.B., Mendrola, J.M., Cho, H., Leahy, D.J., and Lemmon, M.A., in 2003 in a paper entitled "EGF activates its receptor by removing interactions that auto-inhibit ectodomain dimerization" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2003.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely epidermal growth factor receptor and epidermal growth factor.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms heterodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 2 unique UniProt proteins: