1M6B

Structure of the HER3 (ERBB3) Extracellular Domain

Summary for 1M6B

• Entry DOI: 10.2210/pdb1m6b/pdb
• Descriptor: Receptor protein-tyrosine kinase erbB-3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: tyrosine kinase; cell surface receptor; immunity, signaling protein, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 140573.66

Authors

Leahy, D.J.,Cho, H.-S. (deposition date: 2002-07-15, release date: 2002-08-02, Last modification date: 2024-10-30)

Primary citation

Cho, H.S.,Leahy, D.J.
Structure of the extracellular region of HER3 reveals an interdomain tether.
Science, 297:1330-1333, 2002

PubMed Abstract: We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family. The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor. The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling. These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.

PubMed: 12154198
DOI: 10.1126/science.1074611

Experimental method

X-RAY DIFFRACTION (2.6 Å)