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1bmp

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(New page: 200px<br /> <applet load="1bmp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bmp, resolution 2.8&Aring;" /> '''BONE MORPHOGENETIC P...)
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'''BONE MORPHOGENETIC PROTEIN-7'''<br />
'''BONE MORPHOGENETIC PROTEIN-7'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1BMP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BMP OCA].
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1BMP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMP OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Griffith, D.L.]]
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[[Category: Griffith, D L.]]
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[[Category: Scott, D.L.]]
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[[Category: Scott, D L.]]
[[Category: bone]]
[[Category: bone]]
[[Category: cartilage]]
[[Category: cartilage]]
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[[Category: transforming growth factor]]
[[Category: transforming growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:52 2008''

Revision as of 09:56, 21 February 2008


1bmp, resolution 2.8Å

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BONE MORPHOGENETIC PROTEIN-7

Overview

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.

About this Structure

1BMP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily., Griffith DL, Keck PC, Sampath TK, Rueger DC, Carlson WD, Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):878-83. PMID:8570652

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