2BHK

Crystal structure of human growth and differentiation factor 5 (GDF5)

Summary for 2BHK

• Entry DOI: 10.2210/pdb2bhk/pdb
• Related: 1WAQ
• Descriptor: GROWTH DIFFERENTIATION FACTOR 5, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: growth factor, growth differentiation factor, bone morphogenetic factor, hormone-receptor interaction, cystine knot, preformed receptor dimer, cytokine, dwarfism, glycoprotein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 13899.11

Authors

Schreuder, H.,Liesum, A.,Pohl, J.,Kruse, M.,Koyama, M. (deposition date: 2005-01-12, release date: 2005-03-11, Last modification date: 2024-10-09)

Primary citation

Schreuder, H.,Liesum, A.,Pohl, J.,Kruse, M.,Koyama, M.
Crystal Structure of Recombinant Human Growth Differentiation Factor 5. Evidence for Interaction of the Type I and Type II Receptor Binding Sites.
Biochem.Biophys.Res.Commun., 329:1076-, 2005

PubMed Abstract: The crystal structure of human growth differentiation factor 5 (GDF5) was solved at 2.4A resolution. The structure is very similar to the structure of bone morphogenetic factor 7 (BMP7) and consists of two banana-shaped monomers, linked via a disulfide bridge. The crystal packing of GDF5 is the same as the crystal packing of BMP7. This is highly unusual since only 25-30% of the crystal contacts involve identical residues. Analysis of the crystal packing revealed that residues of the type I receptor epitope are binding to residues of the type II receptor-binding epitope. The fact that for both BMP family members the type I and type II receptor-binding sites interact suggests that the complementary sites on the receptors may interact as well, suggesting a way how preformed receptor heterodimers may form, similar to the preformed receptors observed for the erythropoietin receptor and the BMP2 receptors.

PubMed: 15752764
DOI: 10.1016/J.BBRC.2005.02.078

Experimental method

X-RAY DIFFRACTION (2.4 Å)