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1zkz

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(New page: 200px<br /> <applet load="1zkz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zkz, resolution 2.33&Aring;" /> '''Crystal Structure o...)
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caption="1zkz, resolution 2.33&Aring;" />
'''Crystal Structure of BMP9'''<br />
'''Crystal Structure of BMP9'''<br />
==Overview==
==Overview==
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Bone morphogenetic proteins (BMPs), a subset of the transforming growth, factor (TGF)-beta superfamily, regulate a diverse array of cellular, functions during development and in the adult. BMP-9 (also known as growth, and differentiation factor (GDF)-2) potently induces osteogenesis and, chondrogenesis, has been implicated in the differentiation of cholinergic, neurons, and may help regulate glucose metabolism. We have determined the, structure of BMP-9 to 2.3 A and examined the differences between our model, and existing crystal structures of other BMPs, both in isolation and in, complex with their receptors. TGF-beta ligands are translated as, precursors, with pro-regions that generally dissociate after cleavage from, the ligand, but in some cases (including GDF-8 and TGF-beta1, -2, and -3), the pro-region remains associated after secretion from the cell and, inhibits binding of the ligand to its receptor. Although the proregion of, BMP-9 remains tightly associated after secretion, we find, in several, cell-based assays, that the activities of BMP-9 and BMP-9.pro-region, complex were equivalent. Activin receptor-like kinase 1 (ALK-1), an orphan, receptor in the TGF-beta family, was also identified as a potential, receptor for BMP-9 based on surface plasmon resonance studies (BIAcore), and the ability of soluble ALK-1 to block the activity of BMP-9.pro-region, complex in cell-based assays.
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Bone morphogenetic proteins (BMPs), a subset of the transforming growth factor (TGF)-beta superfamily, regulate a diverse array of cellular functions during development and in the adult. BMP-9 (also known as growth and differentiation factor (GDF)-2) potently induces osteogenesis and chondrogenesis, has been implicated in the differentiation of cholinergic neurons, and may help regulate glucose metabolism. We have determined the structure of BMP-9 to 2.3 A and examined the differences between our model and existing crystal structures of other BMPs, both in isolation and in complex with their receptors. TGF-beta ligands are translated as precursors, with pro-regions that generally dissociate after cleavage from the ligand, but in some cases (including GDF-8 and TGF-beta1, -2, and -3), the pro-region remains associated after secretion from the cell and inhibits binding of the ligand to its receptor. Although the proregion of BMP-9 remains tightly associated after secretion, we find, in several cell-based assays, that the activities of BMP-9 and BMP-9.pro-region complex were equivalent. Activin receptor-like kinase 1 (ALK-1), an orphan receptor in the TGF-beta family, was also identified as a potential receptor for BMP-9 based on surface plasmon resonance studies (BIAcore) and the ability of soluble ALK-1 to block the activity of BMP-9.pro-region complex in cell-based assays.
==About this Structure==
==About this Structure==
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1ZKZ 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=1ZKZ OCA].
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1ZKZ 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=1ZKZ OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baker, K.A.]]
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[[Category: Baker, K A.]]
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[[Category: Brown, M.A.]]
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[[Category: Brown, M A.]]
[[Category: Chen, C.]]
[[Category: Chen, C.]]
[[Category: Choe, S.]]
[[Category: Choe, S.]]
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[[Category: signal]]
[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:36:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:36 2008''

Revision as of 14:16, 21 February 2008


1zkz, resolution 2.33Å

Drag the structure with the mouse to rotate

Crystal Structure of BMP9

Overview

Bone morphogenetic proteins (BMPs), a subset of the transforming growth factor (TGF)-beta superfamily, regulate a diverse array of cellular functions during development and in the adult. BMP-9 (also known as growth and differentiation factor (GDF)-2) potently induces osteogenesis and chondrogenesis, has been implicated in the differentiation of cholinergic neurons, and may help regulate glucose metabolism. We have determined the structure of BMP-9 to 2.3 A and examined the differences between our model and existing crystal structures of other BMPs, both in isolation and in complex with their receptors. TGF-beta ligands are translated as precursors, with pro-regions that generally dissociate after cleavage from the ligand, but in some cases (including GDF-8 and TGF-beta1, -2, and -3), the pro-region remains associated after secretion from the cell and inhibits binding of the ligand to its receptor. Although the proregion of BMP-9 remains tightly associated after secretion, we find, in several cell-based assays, that the activities of BMP-9 and BMP-9.pro-region complex were equivalent. Activin receptor-like kinase 1 (ALK-1), an orphan receptor in the TGF-beta family, was also identified as a potential receptor for BMP-9 based on surface plasmon resonance studies (BIAcore) and the ability of soluble ALK-1 to block the activity of BMP-9.pro-region complex in cell-based assays.

About this Structure

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

Reference

Crystal structure of BMP-9 and functional interactions with pro-region and receptors., Brown MA, Zhao Q, Baker KA, Naik C, Chen C, Pukac L, Singh M, Tsareva T, Parice Y, Mahoney A, Roschke V, Sanyal I, Choe S, J Biol Chem. 2005 Jul 1;280(26):25111-8. Epub 2005 Apr 25. PMID:15851468

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