The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors

被引：462

作者：

Garrett, TPJ

McKern, NM

Lou, MZ

Elleman, TC

Adams, TE

Lovrecz, GO

Kofler, M

Jorissen, RN

Nice, EC

Burgess, AW

Ward, CW

机构：

[1] Royal Melbourne Hosp, Walter & Eliza Hall Inst Med Res, Parkville, Vic 3050, Australia

[2] Royal Melbourne Hosp, Cooperat Res Ctr Cellular Growth Factors, Parkville, Vic 3050, Australia

[3] Royal Melbourne Hosp, Ludwig Inst Canc Res, Parkville, Vic 3050, Australia

[4] CSIRO Hlth Sci & Nutr, Parkville, Vic 3052, Australia

来源：

MOLECULAR CELL | 2003年 / 11卷 / 02期

关键词：

D O I：

10.1016/S1097-2765(03)00048-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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.

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收藏

页码：495 / 505

页数：11

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