1TGK

HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000

Summary for 1TGK

• Entry DOI: 10.2210/pdb1tgk/pdb
• Descriptor: TRANSFORMING GROWTH FACTOR BETA 3 (1 entity in total)
• Functional Keywords: growth factor, mitogen, glycoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P10600
• Total number of polymer chains: 1
• Total formula weight: 12734.50

Authors

Mittl, P.R.E.,Priestle, J.P.,Gruetter, M.G. (deposition date: 1996-07-10, release date: 1997-03-12, Last modification date: 2024-11-20)

Primary citation

Mittl, P.R.,Priestle, J.P.,Cox, D.A.,McMaster, G.,Cerletti, N.,Grutter, M.G.
The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding.
Protein Sci., 5:1261-1271, 1996

PubMed Abstract: Transforming growth factors beta belong to a group of cytokines that control cellular proliferation and differentiation. Five isoforms are known that share approximately 75% sequence identity, but exert different biological activities. The structure of TGF-beta 3 was solved by X-ray crystallography and refined to a final R-factor of 17.5% at 2.0 A resolution. Comparison with the structure of TGF-beta 2 (Schlunegger MP, Grütter MG, 1992, Nature 358:430-434; Daopin S, Piez KA, Ogawa Y, Davies DR, 1992, Science 257:369-373) reveals a virtually identical central core. Differences exist in the conformations of the N-terminal alpha-helix and in the beta-sheet loops. In TGF-beta 3, the N-terminal alpha-helix has moved approximately 1 A away from the central core. This movement can be correlated with the mutation of Leu 17 to Val and Ala 47 to Pro in TGF-beta 3. The beta-sheet loops rotate as a rigid body 9 degrees around an axis that runs approximately parallel to the dimer axis. If these differences are recognized by the TGF-beta receptors, they might account for the individual cellular responses. A molecule of the precipitating agent dioxane is bound in a crystal contact, forming a hydrogen bond with Trp 32. This dioxane may occupy a carbohydrate-binding site, because dioxane possesses some structural similarity with a carbohydrate. The dioxane is in contact with two tryptophans, which are often involved in carbohydrate recognition.

PubMed: 8819159

Experimental method

X-RAY DIFFRACTION (3.3 Å)