COOPERATIVE DOMAINS IN FIBRONECTIN

被引：21

作者：

TATUNASHVILI, LV

FILIMONOV, VV

PRIVALOV, PL

METSIS, ML

KOTELIANSKY, VE

INGHAM, KC

MEDVED, LV

机构：

[1] AMER RED CROSS, BIOMED RES & DEV, BIOCHEM LAB, ROCKVILLE, MD 20855 USA

[2] ACAD SCI USSR, INST PROT RES, PUSHCHINO, USSR

[3] ACAD MED SCI USSR, CARDIOL RES CTR, MOSCOW 109801, USSR

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1990年 / 211卷 / 01期

关键词：

D O I：

10.1016/0022-2836(90)90018-H

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：

The melting of human plasma fibronectin and its proteolytic fragments has been studied by scanning microcalorimetry to reveal co-operative structural domains in the molecule. It has been established that each of the two similar polypeptide chains of fibronectin has at least 12 structural domains, which differ in stability, size and function. Many of the domains in the N-terminal half of the polypeptide chains appear to be composed of two homologous repeat modules that co-operate to form a single co-operative unit. In the intact fibronectin molecule, the C-terminal regions of both chains seem to interact forming a stable co-operative block. © 1990.

引用

页码：161 / 169

页数：9

共 45 条

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