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Crystal Structure of Transforming Growth Factor-β2: an Unusual Fold for the Superfamily
Abstract
The transforming growth factors-β (TGF-β1 through -β5) 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-β2, has been determined at 2.1 angstrom (Å) 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 Å by 20 Å by 15 Å. 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-β superfamily, including the activins, inhibins, and several developmental factors, imply that they also adopt the TGF-β fold.
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Cited by
Double muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039
TGF-β and the TGF-β family: context-dependent roles in cell and tissue physiology
Morikawa, M., Derynck, R., & Miyazono, K. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021873 · Cited by 1,321
Latent TGF-β structure and activation
Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013
REGULATION OF MUSCLE MASS BY MYOSTATIN
Lee, S.-J. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.135836 · Cited by 819
Specificity, versatility, and control of TGF-β family signaling
Derynck, R., & Budi, E. H. (2019) · Science Signaling · doi:10.1126/scisignal.aav5183 · Cited by 785
Metadata
- Authors
- Daopin, S., Piez, K. A., Ogawa, Y., & Davies, D. R.
- Venue
- Science
- Published
- 1992-07-17
- Volume
- 257
- Issue
- 5068
- Pages
- 369-373
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2044440492
- Cited by
- 440
- References
- 0
- FWCI
- 11.83
- Type
- journal article
- Language
- en
- Open access
- closed
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- Daopin, S., Piez, K. A., Ogawa, Y., & Davies, D. R. (1992). Crystal Structure of Transforming Growth Factor-β2: an Unusual Fold for the Superfamily. Science. https://doi.org/10.1126/science.1631557
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