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1tgk

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(New page: 200px<br /> <applet load="1tgk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tgk, resolution 3.3&Aring;" /> '''HUMAN TRANSFORMING G...)
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Revision as of 17:18, 12 November 2007

Image:1tgk.gif

1tgk, resolution 3.3Å

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HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000

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

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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