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2tgi
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(New page: 200px<br /><applet load="2tgi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2tgi, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 11:57, 21 November 2007
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CRYSTAL STRUCTURE OF TRANSFORMING GROWTH FACTOR-BETA2: AN UNUSUAL FOLD FOR THE SUPERFAMILY
Overview
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.
About this Structure
2TGI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily., Daopin S, Piez KA, Ogawa Y, Davies DR, Science. 1992 Jul 17;257(5068):369-73. PMID:1631557
Page seeded by OCA on Wed Nov 21 14:04:35 2007
