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Structure of the extracellular region of HER3 reveals an interdomain tether.

Cho HS, Leahy DJ
Science 297 1330-3 (2002)
Cited: 256 times
EuropePMC logo PMID: 12154198

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.

Reviews - 1m6b mentioned but not cited (4)

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Articles - 1m6b mentioned but not cited (23)

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Articles citing this publication (157)

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