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Structure paper

TitleEGF activates its receptor by removing interactions that auto-inhibit ectodomain dimerization
Journal, issue, pagesMol. Cell, Vol. 11, Page 507-517, Year 2003
Publish dateJan 21, 2003 (structure data deposition date)
AuthorsFerguson, K.M. / Berger, M.B. / Mendrola, J.M. / Cho, H. / Leahy, D.J. / Lemmon, M.A.
External linksMol. Cell / PubMed:12620237
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-1nql:
Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsHORMONE/GROWTH FACTOR RECEPTOR / cell surface receptor / tyrosine kinase / glycoprotein / endosomal / growth factor / auto-inhibition / HORMONE-GROWTH FACTOR RECEPTOR COMPLEX

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