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重组人骨形成蛋白1的三维结构：转化生长因子β超家族的结构范例

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

作者信息

Griffith D L, Keck P C, Sampath T K, Rueger D C, Carlson W D

机构信息

Rosenstiel Basic Medical Research Center, Brandeis University, Waltham, MA 02254, USA.

出版信息

Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):878-83. doi: 10.1073/pnas.93.2.878.

DOI:10.1073/pnas.93.2.878
PMID:8570652
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC40151/
Abstract

We report the three-dimensional structure of osteogenic protein 1 (OP-1, also known as bone morphogenetic protein 7) to 2.8-A 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 in 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.

摘要

我们报道了成骨蛋白1（OP-1，也称为骨形态发生蛋白7）的三维结构，分辨率达到2.8埃。OP-1是转化生长因子β（TGF-β）超家族蛋白的成员，能够在体内诱导新骨形成。该超家族成员在其C端区域具有序列相似性，并参与胚胎发育和成人组织修复。我们的晶体结构使得对TGF-β超家族两个成员进行结构比较成为可能。我们发现，尽管OP-1和TGF-β2之间的序列同一性有限，但它们共享一个共同的多肽折叠。这些结果为将OP-1/TGF-β2折叠作为整个TGF-β超家族的主要结构基序奠定了基础。对OP-1和TGF-β2结构的详细比较揭示了显著差异，这些差异为了解这些生长因子如何与其受体相互作用提供了线索。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/a8b2e4c75845/pnas01506-0347-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/2b0786f198ca/pnas01506-0343-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/5a000ee8f162/pnas01506-0344-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/fed86ba4afd8/pnas01506-0344-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/05a8c0b1e13f/pnas01506-0345-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/9729ad87e09d/pnas01506-0345-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/a8b2e4c75845/pnas01506-0347-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/2b0786f198ca/pnas01506-0343-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/5a000ee8f162/pnas01506-0344-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/fed86ba4afd8/pnas01506-0344-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/05a8c0b1e13f/pnas01506-0345-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/9729ad87e09d/pnas01506-0345-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9def/40151/a8b2e4c75845/pnas01506-0347-a.jpg

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