1tgk

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[[Image:1tgk.gif|left|200px]]
[[Image:1tgk.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1tgk", creates the "Structure Box" on the page.
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|GENE= HTGF-BETA3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1tgk| PDB=1tgk | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgk OCA], [http://www.ebi.ac.uk/pdbsum/1tgk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tgk RCSB]</span>
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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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[[Category: Mittl, P R.E.]]
[[Category: Mittl, P R.E.]]
[[Category: Priestle, J P.]]
[[Category: Priestle, J P.]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: growth factor]]
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[[Category: Growth factor]]
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[[Category: mitogen]]
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[[Category: Mitogen]]
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[[Category: signal]]
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[[Category: Signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:55:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:44 2008''
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Revision as of 06:55, 3 May 2008

Template:STRUCTURE 1tgk

HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000


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.

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 Page seeded by OCA on Sat May 3 09:55:32 2008

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