1s78
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| , resolution 3.25Å | |||||||
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| Ligands: | , | ||||||
| Gene: | ERBB2, HER2, NGL, NEU (Homo sapiens) | ||||||
| Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
| Related: | 1N8Y, 1N8Z, 1L7I
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
OverviewOverview
We have determined the 3.2 A X-ray crystal structure of the extracellular domain of the human epidermal growth factor receptor 2 (ErbB2 or HER2) in a complex with the antigen binding fragment of pertuzumab, an anti-ErbB2 monoclonal antibody also known as 2C4 or Omnitarg. Pertuzumab binds to ErbB2 near the center of domain II, sterically blocking a binding pocket necessary for receptor dimerization and signaling. The ErbB2-pertuzumab structure, combined with earlier mutagenesis data, defines the pertuzumab residues essential for ErbB2 interaction. To analyze the ErbB2 side of the interface, we have mutated a number of residues contacting pertuzumab and examined the effects of these mutations on pertuzumab binding and ErbB2-ErbB3 heterodimerization. We have also shown that conserved residues previously shown to be necessary for EGF receptor homodimerization may be dispensible for ErbB2-ErbB3 heterodimerization.
About this StructureAbout this Structure
1S78 is a Single protein structure of sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex., Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, Sliwkowski MX, Cancer Cell. 2004 Apr;5(4):317-28. PMID:15093539
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