2TGI

CRYSTAL STRUCTURE OF TRANSFORMING GROWTH FACTOR-BETA2: AN UNUSUAL FOLD FOR THE SUPERFAMILY

2TGI の概要

• エントリーDOI: 10.2210/pdb2tgi/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)
• 細胞内の位置: Secreted: P61812
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12732.60

構造登録者

Daopin, S.,Davies, D.R. (登録日: 1993-10-20, 公開日: 1994-01-31, 最終更新日: 2024-10-16)

主引用文献

Daopin, S.,Piez, K.A.,Ogawa, Y.,Davies, D.R.
Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.
Science, 257:369-373, 1992

PubMed 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 (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.

PubMed: 1631557

実験手法

X-RAY DIFFRACTION (1.8 Å)