From Proteopedia
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| - | [[Image:1tgk.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1tgk.png|left|200px]] |
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| | {{STRUCTURE_1tgk| PDB=1tgk | SCENE= }} | | {{STRUCTURE_1tgk| PDB=1tgk | SCENE= }} |
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| - | '''HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000'''
| + | ===HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000=== |
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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8819159}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8819159 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8819159}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mitogen]] | | [[Category: Mitogen]] |
| | [[Category: Signal]] | | [[Category: Signal]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:55:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:23:46 2008'' |
Revision as of 09:23, 27 July 2008
Template:STRUCTURE 1tgk
HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000
Template:ABSTRACT PUBMED 8819159
About this Structure
1TGK is a Single protein structure of sequence from Homo sapiens. 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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