Structure of the extracellular region of HER3 reveals an interdomain tether

Hyun Soo Cho, Daniel J. Leahy

Research output: Contribution to journalArticle

306 Citations (Scopus)

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
Pages (from-to)1330-1333
Number of pages4
JournalScience
Volume297
Issue number5585
DOIs
Publication statusPublished - 2002 Aug 23

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Epidermal Growth Factor Receptor
Ligands
IGF Type 1 Receptor
Therapeutics

All Science Journal Classification (ASJC) codes

  • General

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Cho, Hyun Soo ; Leahy, Daniel J. / Structure of the extracellular region of HER3 reveals an interdomain tether. In: Science. 2002 ; Vol. 297, No. 5585. pp. 1330-1333.
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Structure of the extracellular region of HER3 reveals an interdomain tether. / Cho, Hyun Soo; Leahy, Daniel J.

In: Science, Vol. 297, No. 5585, 23.08.2002, p. 1330-1333.

Research output: Contribution to journalArticle

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