Three-dimensional structure of recombinant human osteogenic protein 1: Structural paradigm for the transforming growth factor beta superfamily

被引：243

作者：

Griffith, DL

Keck, PC

Sampath, TK

Rueger, DC

Carlson, WD

机构：

[1] BRANDEIS UNIV, ROSENSTIEL BASIC MED SCI RES CTR, WALTHAM, MA 02254 USA

[2] CREAT BIOMOLECULES INC, HOPKINTON, MA 01748 USA

[3] BRIGHAM & WOMENS HOSP, BOSTON, MA 02115 USA

[4] HARVARD UNIV, SCH MED, BOSTON, MA 02115 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1996年 / 93卷 / 02期

关键词：

x-ray crystallography; protein structure; bone morphogenetic protein; cystine knot; receptor binding model;

D O I：

10.1073/pnas.93.2.878

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We report the three-dimensional structure of osteogenic protein 1 (OP-1, also known as bone morphogenetic protein 7) to 2.8-Angstrom resolution. OP-1 is a member of the transforming growth factor beta (TGF-beta) superfamily of proteins and is able to induce new bone formation ira vivo. Members of this superfamily share sequence similarity in their C-terminal regions and are implicated in embryonic development and adult tissue repair. Our crystal structure makes possible the structural comparison between two members of the TGF-beta superfamily. We find that although there is limited sequence identity between OP-1 and TGF-beta 2, they share a common polypeptide fold. These results establish a basis for proposing the OP-1/TGF-beta 2 fold as the primary structural motif for the TGF-beta superfamily as a whole. Detailed comparison of the OP-1 and TGF-beta 2 structures has revealed striking differences that provide insights into how these growth factors interact with their receptors.

引用

页码：878 / 883

页数：6

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