2bhk
From Proteopedia
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==Overview== | ==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 . | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2BHK is a | + | 2BHK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BHK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: preformed receptor dimer]] | [[Category: preformed receptor dimer]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:55:17 2007'' |
Revision as of 11:49, 5 November 2007
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CRYSTAL STRUCTURE OF HUMAN GROWTH AND DIFFERENTIATION FACTOR 5 (GDF5)
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.
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 5 13:55:17 2007
