2a91
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Crystal structure of ErbB2 domains 1-3
OverviewOverview
ErbB2 does not bind ligand, yet appears to be the major signaling partner, for other ErbB receptors by forming heteromeric complexes with ErbB1, ErbB3, or ErbB4. The crystal structure of residues 1-509 of ErbB2 at 2.5 A, resolution reveals an activated conformation similar to that of the EGFR, when complexed with ligand and very different from that seen in the, unactivated forms of ErbB3 or EGFR. The structure explains the inability, of ErbB2 to bind known ligands and suggests why ErbB2 fails to form, homodimers. Together, the data suggest a model in which ErbB2 is already, in the activated conformation and ready to interact with other, ligand-activated ErbB receptors.
DiseaseDisease
Known diseases associated with this structure: Adenocarcinoma of lung, somatic OMIM:[164870], Gastric cancer, somatic OMIM:[164870], Glioblastoma, somatic OMIM:[164870], Ovarian cancer, somatic, OMIM:[164870], Sialidosis, type I OMIM:[608272], Sialidosis, type II OMIM:[608272]
About this StructureAbout this Structure
2A91 is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors., Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Kofler M, Jorissen RN, Nice EC, Burgess AW, Ward CW, Mol Cell. 2003 Feb;11(2):495-505. PMID:12620236
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