STRUCTURE-FUNCTION-RELATIONSHIPS IN EPIDERMAL GROWTH-FACTOR (EGF) AND TRANSFORMING GROWTH FACTOR-ALPHA (TGF-ALPHA)

被引：49

作者：

CAMPBELL, ID ^{[1
]}

BARON, M ^{[1
]}

COOKE, RM ^{[1
]}

DUDGEON, TJ ^{[1
]}

FALLON, A ^{[1
]}

HARVEY, TS ^{[1
]}

TAPPIN, MJ ^{[1
]}

机构：

[1] BRITISH BIOTECHNOL,OXFORD OX4 5LY,ENGLAND

来源：

BIOCHEMICAL PHARMACOLOGY | 1990年 / 40卷 / 01期

关键词：

D O I：

10.1016/0006-2952(90)90175-K

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The solution structures of the homologous growth factors human epidermal growth factor (hEGF) and human transforming growth factor-alpha (hTGF-α), as determined by high resolution NMR and various computational methods, are described. Knowledge of these structures and the sequences of other homologous proteins leads to predictions about growth factor residues which may be involved in the receptor/ligand interface. Recent experiments designed to check these predictions are described briefly. These involve site-specific mutagenesis, receptor binding assays and high resolution NMR studies. © 1990.

引用

页码：35 / 40

页数：6

共 29 条

[1]

BARON M, 1989, PROTEIN PRODUCTION B, P49

[2]

BRAKE AJ, 1984, P NATL ACAD SCI-BIOL, V81, P4642, DOI 10.1073/pnas.81.15.4642

[3] CALCULATION OF PROTEIN CONFORMATIONS BY PROTON PROTON DISTANCE CONSTRAINTS - A NEW EFFICIENT ALGORITHM [J].