1tgj: Difference between revisions

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[[Image:1tgj.gif|left|200px]]<br />

[[Image:1tgj.gif|left|200px]]<br /><applet load="1tgj" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1tgj" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1tgj, resolution 2.0Å" />

'''HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE'''<br />

==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.

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==

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==About this Structure==

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].

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==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Gruetter, M.G.]]

[[Category: Gruetter, M G.]]

[[Category: Mittl, P.R.E.]]

[[Category: Mittl, P R.E.]]

[[Category: Priestle, J.P.]]

[[Category: Priestle, J P.]]

[[Category: DIO]]

[[Category: glycoprotein]]

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[[Category: signal]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:21 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1tgj.gif|left|200px]]<br />
+[[Image:1tgj.gif|left|200px]]<br /><applet load="1tgj" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1tgj" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1tgj, resolution 2.0&Aring;" />
 '''HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE'''<br />
 ==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.
+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==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-TGJ 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].
+TGJ 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==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Gruetter, M.G.]]
+[[Category: Gruetter, M G.]]
-[[Category: Mittl, P.R.E.]]
+[[Category: Mittl, P R.E.]]
-[[Category: Priestle, J.P.]]
+[[Category: Priestle, J P.]]
 [[Category: DIO]]
 [[Category: glycoprotein]]
@@ Line 26: / Line 25: @@
 [[Category: signal]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:24:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:21 2008''