Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-23553
Science 1992 Jul 17;2575068:369-73.
Show Gene links Show Anatomy links

Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.

Daopin S , Piez KA , Ogawa Y , Davies DR .


???displayArticle.abstract???
The transforming growth factors-beta (TGF-beta 1 through -beta 5) are a family of homodimeric cytokines that regulate proliferation and function in many cell types. Family members have 66 to 80% sequence identity and nine strictly conserved cysteines. A crystal structure of a member of this family, TGF-beta 2, has been determined at 2.1 angstrom (A) resolution and refined to an R factor of 0.172. The monomer lacks a well-defined hydrophobic core and displays an unusual elongated nonglobular fold with dimensions of approximately 60 A by 20 A by 15 A. Eight cysteines form four intrachain disulfide bonds, which are clustered in a core region forming a network complementary to the network of hydrogen bonds. The dimer is stabilized by the ninth cysteine, which forms an interchain disulfide bond, and by two identical hydrophobic interfaces. Sequence profile analysis of other members of the TGF-beta superfamily, including the activins, inhibins, and several developmental factors, imply that they also adopt the TGF-beta fold.

???displayArticle.pubmedLink??? 1631557
???displayArticle.link??? Science


Species referenced: Xenopus laevis
Genes referenced: tgfb1 tgfb2

References :
Hoffman, Researchers get a first look at the versatile TGF-beta family. 1992, Pubmed