1TFG

AN UNUSUAL FEATURE REVEALED BY THE CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF HUMAN TRANSFORMING GROWTH FACTOR-BETA2

1TFG の概要

• エントリーDOI: 10.2210/pdb1tfg/pdb
• 分子名称: TRANSFORMING GROWTH FACTOR, BETA 2 (2 entities in total)
• 機能のキーワード: growth factor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12732.60

構造登録者

Gruetter, M.,Schlunegger, M. (登録日: 1992-11-17, 公開日: 1993-10-31, 最終更新日: 2024-11-20)

主引用文献

Schlunegger, M.P.,Grutter, M.G.
An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2.
Nature, 358:430-434, 1992

PubMed Abstract: 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.

PubMed: 1641027
DOI: 10.1038/358430a0

実験手法

X-RAY DIFFRACTION (1.95 Å)