Structure of the extracellular region of HER3 reveals an interdomain tether

Hyun Soo Cho, Daniel J. Leahy

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)1330-1333
Number of pages4
JournalScience
Volume297
Issue number5585
DOIs
StatePublished - Aug 23 2002

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Structure of the extracellular region of HER3 reveals an interdomain tether'. Together they form a unique fingerprint.

  • Cite this