Publication Date:
2002-08-03
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Hyun-Soo -- Leahy, Daniel J -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1330-3. Epub 2002 Aug 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12154198" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acid Substitution
;
Animals
;
CHO Cells
;
Cricetinae
;
Crystallography, X-Ray
;
Dimerization
;
Epidermal Growth Factor/chemistry/metabolism
;
Humans
;
Hydrogen Bonding
;
Ligands
;
Molecular Sequence Data
;
Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Receptor, Epidermal Growth Factor/chemistry/metabolism
;
Receptor, ErbB-3/*chemistry/metabolism
;
Recombinant Proteins/chemistry
;
Signal Transduction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
