An unusual feature revealed by the crystal structure at 2.2 resolution of human transforming growth fact or-β2

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摘要：

TRANSFORMING growth factor type β (TGF-β2)is a member of an expanding family of growth factors that regulate prolifer-ation and differentiation of many different cell types. TGF-β2 binds to various receptors, one of which was shown to be a serine/threonine kinase. TGF-β2 is involved in wound healing, bone formationand modulation of immune functions. We report here the crystal structure of TGF-β2 at 2.2 resolution, which reveals a novel monomer fold and dimer association. The monomer consists of two antiparallel pairs of β-strands forming a flat curved surface and a separate, long α-helix. The disulphide-rich core has one disulphide bond 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 β-sheet surface of the other. Four exposed loop regions might determine receptor specificity. The structure provides a suitable model for the TGF-βs and other members of the super-familyand is the basis for the analysis of the TGF-β2 interactions with the receptor.

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Humans Disulfides Transforming Growth Factor beta Recombinant Proteins Crystallography X-Ray Diffraction Protein Conformation Binding Sites Amino Acid Sequence Molecular Sequence Data