2bhk
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN GROWTH AND DIFFERENTIATION FACTOR 5 (GDF5)
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Acromesomelic dysplasia, Hunter-Thompson type OMIM:[601146], Brachydactyly, type A2 OMIM:[601146], Brachydactyly, type C OMIM:[601146], Chondrodysplasia, Grebe type OMIM:[601146], Fibular hypoplasia and complex brachydactyly OMIM:[601146], Multiple synostoses syndrome type 1 OMIM:[601146], Symphalangism, proximal OMIM:[601146]
About this Structure
2BHK is a Single protein structure of sequence from Homo sapiens with IPA as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of recombinant human growth and differentiation factor 5: evidence for interaction of the type I and type II receptor-binding sites., Schreuder H, Liesum A, Pohl J, Kruse M, Koyama M, Biochem Biophys Res Commun. 2005 Apr 15;329(3):1076-86. PMID:15752764
Page seeded by OCA on Mon Nov 12 21:02:44 2007
