1tgj: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1tgj.gif|left|200px]]
{{Seed}}
[[Image:1tgj.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tgj|  PDB=1tgj  |  SCENE=  }}  
{{STRUCTURE_1tgj|  PDB=1tgj  |  SCENE=  }}  


'''HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE'''
===HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE===




==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.
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.
-->
{{ABSTRACT_PUBMED_8819159}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Mitogen]]
[[Category: Mitogen]]
[[Category: Signal]]
[[Category: Signal]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:55:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:19:44 2008''

Revision as of 21:19, 27 July 2008

File:1tgj.png

Template:STRUCTURE 1tgj

HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE

Template:ABSTRACT PUBMED 8819159

About this Structure

1TGJ 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 Mon Jul 28 00:19:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA