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1tfg
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(New page: 200px<br /><applet load="1tfg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tfg, resolution 1.95Å" /> '''AN UNUSUAL FEATURE R...)
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Revision as of 01:06, 21 November 2007
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AN UNUSUAL FEATURE REVEALED BY THE CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF HUMAN TRANSFORMING GROWTH FACTOR-BETA2
Overview
Transforming growth factor type beta 2 (TGF-beta 2) is a member of an, expanding family of growth factors that regulate proliferation and, differentiation of many different cell types. TGF-beta 2 binds to various, receptors, one of which was shown to be a serine/threonine kinase., TGF-beta 2 is involved in wound healing, bone formation and modulation of, immune functions. We report here the crystal structure of TGF-beta 2 at, 2.2 A resolution, which reveals a novel monomer fold and dimer, association. The monomer consists of two antiparallel pairs of, beta-strands forming a flat curved surface and a separate, long, alpha-helix. The disulphide-rich core has one disulphide bone pointing, through a ring formed by the sequence motifs Cys-Ala-Gly-Ala-Cys and, Cys-Lys-Cys, which are themselves connected through the cysteines. Two, monomers are connected through a single disulphide bridge and associate, such that the helix of one subunit interacts with the concave beta-sheet, surface of the other. Four exposed loop regions might determine receptor, specificity. The structure provides a suitable model for the TGF-beta s, and other members of the super-family and is the basis for the analysis of, the TGF-beta 2 interactions with the receptor.
About this Structure
1TFG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2., Schlunegger MP, Grutter MG, Nature. 1992 Jul 30;358(6385):430-4. PMID:1641027
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