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| CRYSTAL-STRUCTURE OF TRANSFORMING GROWTH-FACTOR-BETA-2 - AN UNUSUAL FOLD FOR THE SUPERFAMILY |
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| Author(s): DAOPIN S, PIEZ KA, OGAWA Y, DAVIES DR |
| Source: SCIENCE Volume: 257 Issue: 5068 Pages: 369-373 Published: JUL 17 1992 |
| Times Cited: 300 References: 40 |
| 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 (angstrom) 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 angstrom by 20 angstrom by 15 angstrom. 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. NIDDKD, MOLEC BIOL LAB, BETHESDA, MD 20892 USA
2. NIH, FOGARTY INT CTR, BETHESDA, MD 20892 USA
3. CELTRIX PHARMACEUT INC, SANTA CLARA, CA 95052 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: JD674 |
| ISSN: 0036-8075 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |