1tgj

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(New page: 200px<br /> <applet load="1tgj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tgj, resolution 2.0&Aring;" /> '''HUMAN TRANSFORMING G...)
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[[Image:1tgj.gif|left|200px]]<br /><applet load="1tgj" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1tgj" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1tgj, resolution 2.0&Aring;" />
caption="1tgj, resolution 2.0&Aring;" />
'''HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE'''<br />
'''HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE'''<br />
==Overview==
==Overview==
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Transforming growth factors beta belong to a group of cytokines that, control cellular proliferation and differentiation. Five isoforms are, known that share approximately 75% sequence identity, but exert different, biological activities. The structure of TGF-beta 3 was solved by X-ray, crystallography and refined to a final R-factor of 17.5% at 2.0 A, resolution. Comparison with the structure of TGF-beta 2 (Schlunegger MP, Grutter MG, 1992, Nature 358:430-434; Daopin S, Piez KA, Ogawa Y, Davies, DR, 1992, Science 257:369-373) reveals a virtually identical central core., Differences exist in the conformations of the N-terminal alpha-helix and, in the beta-sheet loops. In TGF-beta 3, the N-terminal alpha-helix has, moved approximately 1 A away from the central core. This movement can be, correlated with the mutation of Leu 17 to Val and Ala 47 to Pro in, TGF-beta 3. The beta-sheet loops rotate as a rigid body 9 degrees around, an axis that runs approximately parallel to the dimer axis. If these, differences are recognized by the TGF-beta receptors, they might account, for the individual cellular responses. A molecule of the precipitating, agent dioxane is bound in a crystal contact, forming a hydrogen bond with, Trp 32. This dioxane may occupy a carbohydrate-binding site, because, dioxane possesses some structural similarity with a carbohydrate. The, dioxane is in contact with two tryptophans, which are often involved in, carbohydrate recognition.
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Transforming growth factors beta belong to a group of cytokines that control cellular proliferation and differentiation. Five isoforms are known that share approximately 75% sequence identity, but exert different biological activities. The structure of TGF-beta 3 was solved by X-ray crystallography and refined to a final R-factor of 17.5% at 2.0 A resolution. Comparison with the structure of TGF-beta 2 (Schlunegger MP, Grutter MG, 1992, Nature 358:430-434; Daopin S, Piez KA, Ogawa Y, Davies DR, 1992, Science 257:369-373) reveals a virtually identical central core. Differences exist in the conformations of the N-terminal alpha-helix and in the beta-sheet loops. In TGF-beta 3, the N-terminal alpha-helix has moved approximately 1 A away from the central core. This movement can be correlated with the mutation of Leu 17 to Val and Ala 47 to Pro in TGF-beta 3. The beta-sheet loops rotate as a rigid body 9 degrees around an axis that runs approximately parallel to the dimer axis. If these differences are recognized by the TGF-beta receptors, they might account for the individual cellular responses. A molecule of the precipitating agent dioxane is bound in a crystal contact, forming a hydrogen bond with Trp 32. This dioxane may occupy a carbohydrate-binding site, because dioxane possesses some structural similarity with a carbohydrate. The dioxane is in contact with two tryptophans, which are often involved in carbohydrate recognition.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1TGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with DIO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TGJ OCA].
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1TGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=DIO:'>DIO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGJ OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Gruetter, M.G.]]
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[[Category: Gruetter, M G.]]
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[[Category: Mittl, P.R.E.]]
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[[Category: Mittl, P R.E.]]
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[[Category: Priestle, J.P.]]
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[[Category: Priestle, J P.]]
[[Category: DIO]]
[[Category: DIO]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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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 19:24:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:21 2008''

Revision as of 13:13, 21 February 2008


1tgj, resolution 2.0Å

Drag the structure with the mouse to rotate

HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE

Contents

Overview

Transforming growth factors beta belong to a group of cytokines that control cellular proliferation and differentiation. Five isoforms are known that share approximately 75% sequence identity, but exert different biological activities. The structure of TGF-beta 3 was solved by X-ray crystallography and refined to a final R-factor of 17.5% at 2.0 A resolution. Comparison with the structure of TGF-beta 2 (Schlunegger MP, Grutter MG, 1992, Nature 358:430-434; Daopin S, Piez KA, Ogawa Y, Davies DR, 1992, Science 257:369-373) reveals a virtually identical central core. Differences exist in the conformations of the N-terminal alpha-helix and in the beta-sheet loops. In TGF-beta 3, the N-terminal alpha-helix has moved approximately 1 A away from the central core. This movement can be correlated with the mutation of Leu 17 to Val and Ala 47 to Pro in TGF-beta 3. The beta-sheet loops rotate as a rigid body 9 degrees around an axis that runs approximately parallel to the dimer axis. If these differences are recognized by the TGF-beta receptors, they might account for the individual cellular responses. A molecule of the precipitating agent dioxane is bound in a crystal contact, forming a hydrogen bond with Trp 32. This dioxane may occupy a carbohydrate-binding site, because dioxane possesses some structural similarity with a carbohydrate. The dioxane is in contact with two tryptophans, which are often involved in carbohydrate recognition.

Disease

Known disease associated with this structure: Arrhythmogenic right ventricular dysplasia 1 OMIM:[190230]

About this Structure

1TGJ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding., Mittl PR, Priestle JP, Cox DA, McMaster G, Cerletti N, Grutter MG, Protein Sci. 1996 Jul;5(7):1261-71. PMID:8819159

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