THE STRUCTURAL BASIS FOR THE SPECIFICITY OF EPIDERMAL GROWTH-FACTOR AND HEREGULIN BINDING

被引：99

作者：

BARBACCI, EG ^{[1
]}

GUARINO, BC ^{[1
]}

STROH, JG ^{[1
]}

SINGLETON, DH ^{[1
]}

ROSNACK, KJ ^{[1
]}

MOYER, JD ^{[1
]}

ANDREWS, GC ^{[1
]}

机构：

[1] PFIZER INC,CENT RES,GROTON,CT 06340

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1995年 / 270卷 / 16期

关键词：

D O I：

10.1074/jbc.270.16.9585

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：

Heregulin is a ligand for the erbB3 and erbB4 receptors, with a region of high homology to epidermal growth factor (EGF). Despite this homology, these ligands bind to their corresponding receptors with great specificity. We report here the synthesis of heregulin beta 177-241 and show that a region consisting of amino acids 177-226 is sufficient both for binding and stimulation of receptor phosphorylation. Studies of chimeric EGF/heregulin peptides revealed that amino acids 177-181 of heregulin provide the specificity for binding to the heregulin receptor. The substitution of amino acids 177-181 of heregulin for the N terminus of EGF produced a unique bifunctional agonist that binds with high affinity to both the EGF receptor and the heregulin receptor.

引用

页码：9585 / 9589

页数：5

共 24 条

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[2]

CARRAWAY KL, 1994, J BIOL CHEM, V269, P14303

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